Biomolecules ew sand ld strand (QWECTIVES sug Unt, you wl be able enamocs cahan 1 ay eatofyates, pots, mle acs, vita ard cash cadet. epat and ets |. non ittronce between ONA nd RUA || appreciate the role of these. biomolecules in biosystem. Gi INTRODUCTION Allliving systems need matter as well as energy ia one form or the other for their growth and iintenance, The bodies of living systems ¢2f pe ‘enpared to factories. Just as factories Feat fuels heap ad erage fe aaa ilsation of energy, the living systems elf oe fuels and machines. Food constitutes fuel chines. ‘sings and enzymes act as ™a constituents of food are carbohydrates, fats and proteins. ‘The enzymes help in the conversion of food into body parts through the series of chemical processes which are also called biochemical reactions. Most of the biochemical reactions take place in dilute solutions (pH-7) at body temperature (-87°C) and at one ‘atmospheric pressure. Biochemical reactions take place at high speed and are highly selective. The branch of eience that deals with the study of the chemical composition and the structure of living organisms dnd also various chemical changes taking place tuithin them is called biochemistry. The complex fnganie molecules such as carbohydrates, proteins, Fins, nucleic acids ete, which form the basis of life, in. which build up living organisms and are also veined for their growth and maintenance are called Tinmotecules. Biomolecules are related to the living crganisms in the following sequence ‘Living Organism > Organs -> Tissues ~ Cells 5 Organelles + Biomolecules. In this unit, we shall study the structure and function of some ofthe important biomolecules, Scanned with CamScanner806 ‘Tho cellis the fundamental unit of small to be seen with the naked eyes, However, it ean be seen with the help of microscope, Cells are packets of chemicals essential for life. The most important characteristic of the cell is its ability to grow and divide to produce celts. These daughter cells ean further divide rduce new progeny of cells, Cells may he combined m tissues; tissties may be prouped into organs: and organs may be combined into arganisms. A typical ‘animal cell is described diagrammatically in Alivingcell contains about 50 elements, The 11 most abundant elements in living organisms are 0, C,H, Ny Ca, PK. S. Cl. Na and Mg. The first four elements oxyen, carbon, hydrogen and nitrogen together account for 96% of man’s total mass. The most abundant substance ina living cell is water which amounts to about 70° of the weight. In addition to water, the cell contain a large number of earbon compounds. These compounds can be divided into two classes. The compounds of first class are smal! molecules having molecular masses in the range of 100 to 1000 and containing up to 30 carbon. atoms. These are found free in solution in the cytoplasm of the cell. They form a number of intermediates from which the molecules belonging to the second class are synthesised. Extracellular matrix Mitochondria Plasma membrane Endoplasmic reticulum Fig, 14.1. Structural components of a cell. ‘The compounds of the second class are macromol- ecules. Among these, the most important are: carbohy. rates, proteins, lipids and nucleic acids, CARBOHYDRATES Carbohydrates constitute an important class of compounds like glucose, fructose, sucrose, starch, cellulose, etc., which play a vital role in our everyday ~~ Comprchontiee gy Carbohydrates are also known as eq, Caeally the name carbohydrate was reatide, compounds pertaining to general formula Gf)” they wore considered tobe hydrates ofearben, fo 2% thie definition could not hold ground for on flowing remo ; i) Many compounds like formaldehye, : 2 acid (C,H,0,), ete. ,eanforn is iho, €,(H1,0), but they do not exhibit the egal teristic properties of carbohydrates, (id Some carbohyedrates ike rhamnose (Co deoxyribose (C:K90,) do not conform ty formula C,(H,0),, and e (iif) Carbon is not known to form hydrates, The above facts ultimately gave way to ty, modern definition of carbohydrates. Carbohydr, ae now defined as optically active polyhydrye aldehydes or polyhydroxy ketones or 1k, compounds which can be hydrolysed to them, CLASSIFICATION OF CARBOHYDRATES Carbohydrates are classified into three major categories depending upon their behaviour towards hydrolysis: 1, Monosaccharides These are simple carbohydrates which cannot be hydrolysed to still simpler carbohydrates. About 20 monosaccharides are known to occur in nature. Gluense and fructose are common examples. 2. Oligosaccharides These are the carbohydrates which on hydrolysis give two to ten units of monosaccharides. Accordingl, they may be further divided into di, tri or tetrasa- ccharides depending upon the actual number of monosaccharide units formed by the hydrolysis of particular oligosaccharide. Disaccharides give two units of monosacch- rides on hydrolysis. The two monosaccharide units obtained on hydrolysis of a disaccharide may be same or different. Common examples ar? Sucrose and maltose. Both have molecular formula C,,H,,0,,. Sucrose on hydrolysis gives one molecule of glucose and one molecule of fructose whert®s maltose on hydrolysis gives two molecules glucose only, reve, B due 4), Scanned with CamScanner-enariden give three uni rates wc Hl mtn. 9 examples OCH Ose in pmjcehariden fr unite of “is on hydrolysis. Stachyone, so nin exe CHO, in at pulyseeharies yaeare the carbohydrates whic 7 den We holed to ee large ome er Marie nits, The commonly fe munber Have the general formula (C,,0,). imples are starch, glycogen 5 ted that, the carbohydrates which sesnes mtn ae collectively called sugars hil erepieh are not sweet are called non-ru a ides and disaccharides are aaaase bi ionosce olyoee jurides are non-sugars, ithe relative degree of sweetness of various gars is given below in tabular form: ex aa ee ‘Mal. \Galae-| Glu-| Sue- | Frue- ‘owe | tose | tone | cose | rose | tose ee | | A 173 gweetnest © Do You Ke? —$_<__—_—_— [Tendon carbohydrates, some other ‘compounds are For example, st 550 times as sweet 38 SUTOSS- pout 100 times sweeter for more sweet. Saccharin is abo ‘Aspartame, a peptide, is than sucrose. Suerotose, a trichloroderivative of {G00 times sweeter than SUCTOSS: ates may also reducing sum ‘Tollen’s reagent ing sugars. agents are cal sucrose, is about be classified a5 rs, The carbo- or Febling’s while those led non- ‘The carbohydrt solution are lass ido not reduce ehese Te which reducing sugars , Reducing sugars Conny” free farides are Te roup. AIL monosacehar reducing oF BOM” Disaccharides MAY orn cabo eae! nee ide is non-reducing: ‘avowed in Tinkages (DY nom Onhe other ham ce of te carbony yups is ft the diszechari fugar arin is reducing. Sucro ile maltose is a ose is a non-reducing reducing sugar. IONOSACCHARIDES As pointed carbohydrates roles earlier, these are the simp Soe be hydrolysed to give aldehyde ohydrates. Monosaccharides containing eu talled aldoses while those ince ean rae are called ketoses. They ca ssified into different categories depend ent categories depending upon the number of carbon atoms. For inne called an with three carbon atoms: are Monosaccharides with four sare sated mee swith four carbon atoms ar ‘Monosaccharides with five, six and seven carbon, atoms are called pentoses, hexoses 24 eptoses respectively. Table 14.1. Different Types of Monosaccharides Carbon | General | Aldehsde Batone bs ‘Atoms Term 3 sass | assoc | Bares 4 Trost | ‘atdoetrose | Reeters.| 5 Pentose ‘Sidopentose | Ketopentose | 6 Hexose Aldobexose | Ketobexose | 7 Heptose ‘Aldobeptose | Retobeptose | Gome examples of various S7PC® of monosac- charides are being given below: cH cHO cH,OH { 1 H-C-0H H-0-Ol1 G=0 abo CH,OH CHO LOH Giyceraléehyde Dibydresvacrtont Exytbrove “aldose sean) Ate) Ho cH,OH 1 GEO, H—C—OH ° 1 H-C—OH Ho—C—H Ho—C—H U H—c—O# —0—OH H—C—OH 1 oe HOH H—C—OH CH,OH CH,OH CH,OH, Rise huewe —— tatdopentos) aldoberose) —— Betobexose) Scanned with CamScannerecharide \eor more tainon! hexoses contain jie. optically On carefully examining the molecules, we can realise that they cont chiral carbon atoms, For example, aldo four chiral earbons and therefore, (2)', active isomers should be po cHo wocn,-éu—en—en—¢ f OH OH OH OW Thre ofthese sinter aldohernen whieh oct widely in nature are D-glucose, D-galactose and D-mannose whose open chain structure formulae are given as follows: 1 cHo al H—C—OH al Ho—C—H DiGi Decalactose D Mannose D- and L-Notations ‘The letter D before the name of monosaccharides does not refer to dextrorotatory, but represents the con figuration as derived from glyceraldehyde. Glyceral- dehyde can be represented by two enantiomers as shown below as Fischer structures: cHO CHO H OH HO: H CH,OH CH,OH (0)yerldhyde Gieerataedyde By convention a monosaccharide is given a D-configuration if hydroxyl group attached to the carbon adjacent to —CH,OH is on right hand side. On the other hand, it is assigned L-configuration if hydroxyl group attached to the carbon adjacent to —CH,OH is on left hand side, Thus, (#)-glyceraldehyde has D-configuration while (~)-glyceraldehyde has L-configuration. All those £ SASTRY eh | “da which can be chemically corre, said to possess D-co to dehyde are #3 mia ich can be correlated to tin .aa L-configuration. ve compoun co-lyeceral ‘phile those whi to posse’ ; Taner tonssign thecontisuration ofa mo he lowest aaymmettic carbon ator 'e example, in (+)-glucose, OH, ‘ymmetric carbon is on the right ya? i NOsae, Which fon the lowest a post ore Therefore, -Rtucose is assizmed D-configuraynn CHO "1 ee cHo toa on H—— on it qakagh CH,OH cHon ielyoradehyde Deluca GLUCOSE (DEXTROSE), CoH,,0, ae Glucose occurs in nature in free state as well as in combined state. In free state, it occurs in sweet fruits ‘and honey. Ripe grapes contain ~ 20% glucose and hens the name grape sugar. In combined state, glucose ig present in di-and polysaccharides. Maltose and starch on hydrolysis yield only glucose. PREPARATION OF GLUCOSE 1. From Sucrose (Cane-sugar). In laboratory, glucose can be prepared by hydrolysis of cane-sugar in the presence of alcohol using dilute hydrochloric acid. Glucose and‘fructose are formed in equal amounts. Glucose, being less soluble in ethyl alcohol than fructose, crystallizes out. C,Hyy0,, + HO —E 4 CgHy0¢ + gH 20 Sco © Prete 2. From Starch. Glucose is obtained, on commercial scale, by hydrolysis of starch by boiling it with dilute sulphurie acid at 393 K under a pressure of 2-3 bar. (CH,)05), +nH,0 ——*__, n0,Hy,0, Starch BOK2Sber Chace STRUCTURE OF GLUCOSE Glucose is an aldohexose. Itis monomer of many of the larger carbohydrates such as starch, cellulose. Scanned with CamScanner allary secondary ri st EON Glucose was assigned the ge (CHOH)s CH,OH peienee® that Support the Structure of pe molecular formu of glucose is WHO, Te eion- Goze is reduced to-sorbitol, a poi aol oP reaction with hydrogen in the ie ent ick ‘as catalyst or on reaction with sodium oo jn aqueous solution. 6 HOH,C - (CHO), * CHO +H, Glucose ie OCH, ~ (CHOH), * CH,OH sortitl suneaction with Hydrogen Todide, iucoseon _einged heating with HI gives n-hexane. HOCH,—(CHOH),—CHO ‘This reaction suggests that the six carbon atoms inglucose are linked linearly. 4, Oxidation. (i) Glucose on oxidation with mild sidising agents, such as bromine watery ‘Tollen’s reagent or Fehling’s solution gives HOCH, - (CHOH), cHO + [0] Gacose gluconic acid. | sea HOCH, - (CHOH), - COOH Guconie acid This confirms the presence of 0 aldehydic grouP- elucose. feagent glucose gives silver mits while Feblng solution and Benedict’ solution, Precipitates of cuprous oxide. HOH,C—(CHOH) CHO + A#0 HOH,C—(CHOT,—COOH + 24% saver mitror Hoctt,-(cHoH,—CHO + 260008): | HOCH,—(CHOH,—COOH + x0, +2420 g agents such as concen” ve glucose as well 2 ‘cid (saccharic acid) (ii) Stronger oxidizint trated nitric acid oxidi gluconic acid to glucaric HOCH, : (CHOH),* cHO + [0] ‘cane. HNOs HOOC - (CHOH), - COOH Clucarie acid Sacthare 21) ‘Thisindicates the presence of Primary aleoholic (OH) group in glucose. 5, Acetylation. When glucose 1s reacted with acetic anhydride in the presence of ‘sulphuric acid, @ pentaacetyl derivative of glucose is obtained. QHC : (CHOH), - CH,OH + 54c,0 A Glucose (hee cH,co OHC - (CHOAG), * CH,OAC Pentaacety! xlucoee acetyl derivative indicates the glucose molecule. Glucose reacts with ce of alkali to form Formation of penta: ence of five OH groups in 6. Ether Formation. «dimethyl sulphate in the presen penta-O-methyl derivative, TOH,C (HOH), - CHO + (CH3)2 SOx Je H,COCH, - (CHOCH,), » CHO Peatarethylelucose 7. Reaction with Hydroxylamine, Glucose reacts with hydroxylamine to give monoxime, Scanned with CamScanner7 Conprcente gy ‘a. 0 is treated with ait G9 When glucose is ate eo DCH,—(CHOH),—-CHO + NH,O11 srenofution, it undergoes 9 "6, ¢%y meet dy dronit resulting in the formation ofq vty Bethtcone, D-fructose and D-mannose, This ee reaction HOCH,—(CHOW,—CH = N—OH + 10 own ae Lobey de Brayo-van’ ehongt Chere ei Marrangement. === D-Mannose <——s 8 Formation of Cyanohydrin, Glucose 0 D.tiucone — falliial aren tre reaction with drogen cynnide gives eyanniyirin, | I ihecus of Que eons Wat Ducts | | Hydrolysis of heeyanohydrin and reduction of the acid] reducon Tori door not eotcmin || obtained with hydrogen iodide yields heptanoie acid. isatste Go. ys) ou ou ~ es : aes - On the basis of its reactions glucose hag py j PHO) TN en J" coon assigned n straight chain structure, ae | wcHom, 2s CHom, Ley (CHOM, ‘The exact spatial arrangement of different, ‘ I rroups was given by Fischer after studying many ap" CHOW CHO CH,OH properties. Its configuration is correctly representer ‘lucene yanahydrin Peale I. Therefore, gluconic acid is represented as {1 a saccharic acid as IIT, uci x0 goon The reactions of glucose with HCN and H- OH Ht on hydroxylamine confirm the presence of a carbonyl group HO: H HO: H in glucose molecule. H OH H- On 2 H OH H oH © Reoudedge Plus CH,OH CH,OH 1 1 Some Typical Reactions of Glucose D.-Glucese Gluconi cid 1. Formation of Osazone. Glucose on reaction with phenyl hydrazine forms phenyl hydrazone. COOH However, when warmed with excess phenyl hydrazine, each glucose molecule reacts with three molecules of H—)— 0H phenylhydrozine and yields osazone. HO—+—-H cHO CH=N-NHCgHs H—— 0H u ! —}— 0H CHOH ¢,H,NHNH, CHOH s 1 = ! CooH (CHOP aa (CHOHD, m éa,o8 _ Soccharie acid CH,NHNH, | ~CgH,NH, Glucose is correctly named as D-(#)-Glucose..D" | Ceuit? | before the name of glucose represents the configuration oy whereas ‘(+)’ represents dextrorotatory nature of the CH=N. NHCGH, GHSN-NHGHe / molecule: C= C=N.NHCGH canst CYCLIC STRUCTURE OF GLUCOSE (CHOH), ~~ (CHOH)s ‘The open chain structure of glucose, could explain ji 1 most of its properties, but failed to explain the following CHO CH,OH properties: Glucosazone 1, Inspite of the presence of an aldehydic group, 2. Reaction with NaOH. (i) When glucose is slucose does not restore the pink colour of Sehils heated with concentrated solution of sodium hydroxide Foadent, does not give 2, 4-DNP test and does not it first turns yellow, then brown and finally resinifies, form addition products with sodium hydrogen sulphite and ammonia, Scanned with CamScannerpentaacetate does not react with icating the absence of fr hydroxyl ee -CHO was jlucos glucose crystallized from y, when i Mpeentrated ethanolic solution at 30% form having melting point 146°C ci it gives tation +111°, On the other hand, eee From hot pyridine gives B-form having re ng a Fein 150°C and specifi rotation +19 fynen either of the &- or B-form At : of i Sstved in water and allowed to atthe aiff rotation changes slowly and attaing an are jlbrium value of + 52.7°, a The spontaneous change of specific rotati : : i iran optically active compound cana or librium value is called mutarotation. When dry hydrogen chloride gas is passed through a solution of glucose in methyl alcohol, a ihren takes place and a mixture of methyl Fefrglucoside and methyl -D-elucoside is ed. These glucosides do not reduce Febling’s solution and also do not react with HCN and hydroxylamine. ‘This indicates that glucosides do not have free —CHO group. ¢ formation of glucosides only one )H combines with a molecule of glucose. ose can be explained e. The cyclic During th molecule of CHO) ‘The above facts about gluc in terms of cyclic structure of glucosi HO—>—# cH,OH yo——#t xt cH,OH H—}— OH H— OH H—}— 08 = | yon un py of glucose Hoong eta formation which leads to cy« Cena ao eisamee veture consisting of five: carbon atoms oe age a ing structure of five carbon atoms and pace hell called pyranose ring. It gets its similar way, the heterocyclic compound pyran In the ay, the ring structure consisting of four car0% atoms and o: A ms and oxygen atom is called furanose 1m analogy with furan. 0 90 0" ‘0 Pyran arse he carbonyl carbon, ‘As a result of cyclization # G1 aleo becomes chiral carbon atom and has two possible arrangements of H and OH grits ‘around it These two arrangements of glucose which differ only jn the orientation of hydroxy! groups at C—1 are calles anomers and are represented as ‘o-D-glucose am B.D-glucose. The earbon C—1 'S called anomeric carbon atom. ‘These two forms of glucose (a-D-glucose and {sD-glucose) are stereoisomers but 9° not mirror image peryach other. Hence, these are not enantiomers but gre dinstereomers: The six “nembered cyclic structure of glucose was established by RD. Haworth. «, ¢H,08 o-D-(4)-Glucose GH,OH 0 p-D-(4)-Glucose Haworth structures Fischer projection formulae Scanned with CamScannerMutarotation can be accounted for by considering the gradual conversion of either form of glticoxe in aqueous solution into other till an equilibrium mixture is formed. This process of conversion of one anomeric form of ghicose into the other in aqueous solution occurs through the open chain structure, The equilibr mixture also contains a small amount of open ch form. For example, ©D-Glucose === Open chain form Specific FRUCTOSE (LAEVULOSE), C,,,0, Fructose is ketohexose.Itis obtained along with slucose by the hydrolysis of sucrose. STRUCTURE OF FRUCTOSE Fructose has the molecular formula C,H, 0, and on the basis of its reactions it was found to contain a ketonic functional group at C—2 and six carbon atoms in straight chain as in case of glucose. It belongs to D-series and is a laevo-rotatory compound. Therefore, fructose is correctly named as D-(-)-fructose. Its open chain structure may be written as: CH.OH c=0 Ho—|—H H—}— 0H H—j— 0H CH,OH DOFructose Fructose also exists in two cyclic forms which are obtained by theaddition of —OH at C—5 to the ( SC = 0) group. The ring, thus formed is a five membered ring and is named as furanose with analogy to the compound furan, 1 I HOH,C—C—OH HO—C—CH,OH Ho—t—H 0 Ho—}—-H oO HS on | u——on Hu HS dl al CH,OH CH,OH a-D-()-Pructofuranose D-(}ructofuranose 4 Comments ai, ‘no eeie trees of to anomery ogy | aro represented by Haworth structures ag gi none OH H BDA) Pructofuranote 14.4 | DISACCHARIDES These are the carbohydrates which give two unt of monosaccharides on hydrolysis with dilute acids s enzymes. Some examples are: ane CypHy90y, ——> CQH,0, + C,H.,0, Sucrose Guctee rane Hom’ CigH2201, ——> CoH 20, + C,H, Tactose Gatacione 20, Hom C,gH,,0,; —— 2C,H,,0, Maltoce Glucose This implies that a disaccharide is formed by condensation of two monosaccharide units. The two monosaccharide units in a disaccharide are joined together by an oxide (or ether) linkage formed by loss of a water molecule, Such a linkage between tno ‘monosaccharide units through oxygen atom is called glycosidic linkage, Now, let us study about some disaccharides in somewhat details. SUCROSE (CANE-SUGAR), C,,H,,0,, Sucrose is the most widely occurring disaccharide. It is found in all photosynthetic plants- It is obtained commercially from sugarcane o sugarbeets. Its aqueous solution is dextrorotatory with | Scanned with CamScanner2. On hydrolysis wi jon + 66.5 lysis with a; wtttase, 1 mole Of sucrose eae acids sah 1 mole of (D)--)-fructoge, | Mle of = tts —> Cotas + CuH,, DeHrelucose D.C. fructn ose 88 non-reducing sugar, . gut | xoses must have joined ial involving C—1 of oath 8 yal ctose AB result, the reducing groups Fe tyr tose are involved in the formation of and ge and hence sucrose bel weimore on jence sucrose behaves as a non. t. st est ; seth COED staeste the following sey. ose asi ‘ fy,08 eo. Tt indieatos | ve i ( OH OH P-D-Fructose unit prGucose ped to Your Ruowoledge —__ suerose is dextrorotatory with specific rotation {465% On hydrolysis in the presence of HCl or enzyme jnerse it produces mixture of D-(+)-glucose (specific tation + 52.7°) and D-(-)-fructose (specific rotation 92.4"). Since specific rotation of D-- fructose is neater than D-(+)-glucose, the resulting solution tomes laevorotatory. As hydrolysis produces change inoptical nature from dextrorotatory to laevorotatory, ihe process is called inversion of sugar. The mixture «fD4(+)-glucose and D-(-)-fructose obtained as a result «hydrolysis is called invert sugar. It may be noted thathoney is mostly invert sugar: ‘as bees produce enzyme inverts «aS ‘When starchis hydrolysed by the enzyme diastase, ‘ultse is formed as one of the products. 4C,H,,0,), +nH,0 =", nCygHs2011 Starch Maltose maltose hvttolysia with dilute acids, one mole of Yields 2 moles of D-(+)-glucose. Cult,0,, 44,0 205 to ie Deglue llores reducing augar, tn maltose thetwo Tinagte nite are linked through dlyeos? 7 trate between C—1 of one lucas unit andl C9 Ee other. The froe aldehyde group can be produced 2° Troy the second glucose in solution. Hence, maltose Shows reducing properties. struct tthe tlucose units are in pyranose fore The ructure of maltose is given below: Chon eD-Glucose unit aeD-Glucose unit Maltose LACTOSE, (MILK SUGAR), C,H. 11 Lactose is present in the milk and is also known as milk sugar. On hydrolysis with dilute acids one mole of lactose yields 1 mole of D-glucose and one mole of D-galactose CygHy,Oyy Vo Ogk05 + Cots Tictce HO” blacore | pD-elactone Lactose is a reducing sugar. In lactose, D-glucose and D-galactose units are Jinked through Beglycosidic linkage between C—1 of galactose and (C—4 of glucose unit. The structure of lactose is given as follows: 6 CH,OH °CH,OH P-D.Glucose unit H on D.Galactse nit a Lactose Scanned with CamScanner \y\ |818 ae POLYSACCHARIDES These are the carbohydrates which are made of large number of monosnecharide units. They are naturally occurring condensation polymors in which large number of monosaccharide units arc joi together through glycosidic linkages. They less, tasteless amorphous powders. They play vital role, in plant and animal life, Let us study the structure of three important polysaccharides starch, cellulose and glycogen. 1, STARCH (AMYLUM), (C,H,,0,), Ttis a most abundant source of earbohydrate in human diet. It is a major food reserve material of plants and occurs mainly in seeds, fruits, tubers and roots of the plants, The important sources of starch are wheat, rice, maize, potatoes, legumes and other vegetables. Starch is the polymer of D(+}-gtucose. It consists of two components : CHLOH a-Glycosidie linkage Comprchenitee CHET (@) Amptose, the water soluble fae finear polymer of D-(+)-hucose yio™* 8d blue colour with iodine. Mme Tei () Amylopectin, the water insoluble f, and consists of linear as well ag yeattion, chain polymers of D-(+)-glucose, ® Natural starch contains approx; 15-20% of amylose and 80- Poo aa pectin. Amylopectin does not give bgt with iodine, A molecule of amyloqc0% contain 200-1000 glucose units where molecule of amylopectin may ert'.2 2000-3000 glucose units. In amylose seit asamylopectin the D-glucose units are yy through c-lyeosidie linkages between get of one glucose unit and C—4 of the | glucose unit. Branching in amylopectin og" through C,~C, glycosidic linkage," | ‘The section of amylose as well amylo been given as follows : ectinhas # CH,OH Amylose (Linear Polymer) CH,OH a-Glycosidic linkage Amylopectin Scanned with CamScannerPr ones. ye hydrolysis with dilute acide or enzymes, svn aon into maltose and finally D-glucose. Diastave aie Tae” CHRO —> Cathe - Maltose D.Giucose pL LULOSE, (CoH 09), 20° collulose occurs exclusively in plants. It is the ‘ ee yet structural material of cell walls of all the ae Its also the chief component of cotton, wood shut. Wood contains 45-50% while cotton contains spundant organie substance in plant kingdom. It f oo-ssteceltulose. It may be noted that over 50% of the ajonganie matter of the living world i ceulose, Cellulose does not reduce Tollen's reagent or Fehling’s solution. It is not fermented by yeast. Cellulose cannot be hydrolysed easily. However, when itis heated with dilute sulphuric acid, under pressure, itundergoes hydrolysis and yields D-glucose. Cellulose forms many useful products when treated with suitable chemical reagents. Some of the important produets are : Celluloid, which is used in films. Gun cotton, which is an explosi Cellulose acetate is used in plastics: for ‘wrapping films and nail polishes- / Methyl cellulose is used in cosmelcs: pastes and for fabric sizing. , . net Ethyl cellulose isused in plastic coats and films. Cellulose 815 Structurally, cellulose is a linear polymer of Deglucose units joined by B-tlycosidic linkage between C=1 of one glucose unit and C—4 of the next glucose ‘The chains are held together by hydrogen bonds between glucose units of adjacent strands. The chains are so arranged as to constitute the bundles. This lends rigidity to its structure, ‘It may be noted that amylose as well as cellulose are formed by condensation of D-glucose units. However, the D-glucose units are joined together, in amylose, by o-glycoside linkage while in cellulose D-glucose units are joined together by Brglycoside linkage. On treatment with concentrated sodium hydroxide, cellulose forms a transluscent mass which imparts a silky lustre to cotton. The process is called mercerisation and cotton so produced is called mercerised cotton. 3. GLYCOGEN Glycogen is the principal reserve of carbohydrates in animals. The molecular structure of glycogen is similar to amylopectin. That is why it is also known as animal starch. However, one main difference between glycogen and amylopectin is that average chain length in glycogen is 10-14 while in amylopectin it is 25-30 glucose units. Glycogen is present in liver, muscles and brain. When the body needs glucose, enzymes break glycogen into glucose. Scanned with CamScannera6 OP ae to Your Keowledge —_— ofother Tnaddition to starch and cellulose, a number polysaccharides are used as food components, These are the gums and pectins. Gums ar polysaccharides made up of more than one type ‘monosaccharides. They are used for thickening and improvement of texture in food industry. Peetins are found in fruit skins and ate extracted by boiling: Jelly preparations contain pectin dissolved ina fruit juice. The pectin causes jelly to set into a semisolid IMPORTANCE OF CARBOHYDRATES The carbohydrates perform many important functions in living bodies 1. They act as biofuels to provide energy for functioning of living organisms. In human system, all the carbohydrates except cellulose can serve as source of energy. Starch and various sugars which are taken as food are first hydrolysed to glucose by the enzymes present in the digestive system. Amylase 2(CgHo0,), + 2H,O ——> nC,.H,, Suarh Matase Matisse ©,2Hy20,, + HO ——— 2C,H,.0, Matose ‘hore Glucose on slow oxidation to carbon dioxide and water in the presence of enzymes liberates large amount of energy which is used by the body for carrying out various functions. C,H,0, + 60, —>+ 6CO, + GH,O + 2832 kJ In order to fulfil the emergency requirements, our body also stores some of the carbohydrates as glycogen in the liver. Glycogen, on hydrolysis, gives glucose. It may be noted that cellulose cannot be hydrolysed in our body because enzymes required for its hydrolysis are not present in our body. However, grazing animals are capable of hydrolysing cellulose to glucose. In these animals cellulolytic bacteria present in the rumen, break down cellulose with the help of enzyme cellulase and is subsequently digested and converted into glucose. Comte ent Cust tituents 2, They act as cons! Of cell ‘me, ofplants and bacteri = 3 Deribose and 2-de0xy-D-ribose gy, cleic acids. inn Carbohydrates are found in boyy, ination ith many protelne and joe combi & Solved Problems a What are reducing and non ugars? What isthe structural feature characterising Stig sugars? ing Solution. Carbohydrates which reduce Tllen's agg, a Falling solution are called reducing sugars, white 0 une glucose, fructose, maltose and Inetose ana Fe sugars while sucrose isa non-reducing sugar, Reducing’? Contain free aldehydic or ketonie group, = Pree Draw open chain structures ‘aldopentose and an aldohexose. How many asymmetric ah ‘are present in cach? Solution. — CHO fas I H—CHOH cat on cae CH,OH H—C—OH Ribose | (Aldopentose) CH,OH Glucose (Aldohexose) There are three asymmetric carbon atoms (markedby asterisk) in aldopentose and four asymmetric carbon atomsia aldohexose, Draw simple Fischer projections of D-and L-glucose. Are these enantiomers? Solution. CHO CHO H OH HO H HO H H ‘OH H Ou HO H H OH HO H CHLOH CH,OH D.Glucose L-Gitucose ‘These are enantiomers, Scanned with CamScannerraw Fischer projections of L-galactose ection formulae of L-galactose and cHo CHO H u—t— on _— OH H—1— 0H oH HO——H 4 HO—+—H cH,OH CH,OH Galactose L-Mannose Amylose and cellulose are both straight EE rectares coming Gly Deglucose units. What pe touctural difference between the two? >, Deglucose units are joined together by ic linkages involving C—1 of one glucose molecule Ge Lofthe nest elucnsy molecule. In cellulose, D-glucose ye are joined together by Beglycosidic linkages between {1 ofone molecule ‘and C4 of the next glucose molecule ee NCERT INTEXT QUESTIONS ‘tion. In amylose, tos Glucose or sucrose are soluble in water bi, ple six membered rine compounds) bpefphexane or benzene (Si v insoluble in water. Explain. .ge and sucrose mole le of fo oH groups and hence are capab! ‘ater molecules. On the other hand, cyelobe ine are hydrocarbons and hence ‘cannot form water. Therefore. Md sucrose are soluble whereas cyclohexane’ zene are not. Solution. Gluco! syles contain many irming H-bonds with sxane and ben= H-bonds with in water ne expected products of What are @ Iydrolysis of lactose? tose o saltioes Tae yarolysis vields Degalactose and Deglucose. in the absence of expla of Dglucose? tspentancetate How do 20! etate se penta _ ve of Deuce exe rou? aldehyde FOP yelie st free aldehyde Solution, Duet? oes not contai® cH.0% at7. 1. Give a 4 ch n example of aldohexose and an aldotriose. 7 ae saa given tothe linkage which holds logeter te ‘monosaccharide units in 3. Out of amylose and amylopect and amylopectin which form of oe What are the functions of carbohydrate ae snydrates in the living 5, Give structures of pyran and furan. 6, Draw structures of o-D-(-) fructo B-D-()-fructo furanose. 4, What are the hydrolysis products of? (Gi) maltose. furanose and ( sucrose FIC OF LAKMT PUBLICATIONS (P) LTD- ‘Awol PROTEINS plex organic substances asm and are found in all rotein (Greek, proteios 19) because Proteins are the com which are the basis of protoP! living organisms. The name Pr sevans firs) was introduced by Mudlar (183 At prime importance of suck substance to animal life. In general, proteins are polymers of camino acids, Like peptides the amino acid units in proteins ate held up by peptide (~CONH-) linkage. In fact, polymeric products of a-aming acids with molecular mass upto 10000 are cal ile those having molecular mass more thai ‘as proteins, However, there is no sharp de! hetween polypeptides and proteins led polypeptides whi 1n 10000 are considered markation ‘AMINO ACIDS ‘These are amino substituted carboss/i¢ acids. Of the camino acids are quite ‘are the building blocks of peptides and proteins. In amino ‘acids, the amino group Pemvesent on the a-carbon atom (Le C atom next to COOH group). Thus, they can be represented by the general formula, the various amino acids, important because they R—CH—COOB. t 12 acAmino acid Group R—is different for different amino acids. rl Scanned with CamScanner818 Comprchensine f most of th 41 as the constituents of on About 20 ofthe camino aids have been iene asthe cone Tiers Do the =, Proteins. All a-amino acids have trivial or common its name from the greek word giyy "Und » Source. For example, glycine is sweet in taste and derives i eo hight ig ah lhe and abbreviated names ch sweet. The formulae of such amino acids along with their common have been trek Table 14.2, ee iy Table 14.2, Structure and Names of Some o-Amino Aci General H,N—CH—COOH ‘Structure 1 R Common Name | Three Letter | One Letter -R ‘Symbol ‘Symbol Neutral amino acids 1. | Glycine Gly a se 2.) Alanine Ala A oe 3. | *Valine Val v —CHCH,), 4. | *Leucine Lew L —CH,—CH(CH,), 5. | *Isoleucine Hew I —CH(CHy)—CH,—CH, 6.] *Phenylalanine Phe F —c,©) 7. | *Methionine Met M —CH,—CH,—S—CH, 8.] *Tryptophane Trp Ww 9. | *Proline Pro P 10. | Serine Ser Ss 11, | Cysteine Cys c —CH,—SH 12. | Aspargine Asn N —CH,—CONH, 13. | Glutamine Gin Q —CH,—CHl,—CONH, 14. | Threonine Thr fr —CH(OH—CH 15. | ‘Tyrosine Tr Y —cHt,©)-on Acidic amino acids 16. | Aspartic acid Asp D —CH,—COOH 17. | Glutamic acid Glu E —CH,—CH,—COOH Basic amino acids 18. | *Lysine Lys K —CH,~(CH,),—NHs" NH,’ 0 19. | *Arginine Arg R —CH,—(CH,),—NH—C—NH, 20. | *Histidine His H cu L | *These are essential amino acids. Scanned with CamScannert10N OF AMINO ACIpg no acids containin am boxy! ETOUPS are peu n and The amino acids whigh 09 ih scit{rboxyl Broups than aming nt jhe Gaic amino acids white the fy hey of amiNO EFOUDS AC called aco™' ining txamples £lulamic acid and qqnt Fe ait? acids while lysine is basie — cia joie eutral amino acid, ino acid, AC! (ist AND NON-ESSENTIAL anni $ ene ja ye of 20 amino acids which are re, ott esis, the human body can | nem hich th ee | oats which the body can ayn (fit essential amino acids, quired for thesize 10, thesise are The remaina af which the Dody is not able 4g nit 10 ja eicesontial amino acids. The essen et” : 1 essential ami ‘ote be supplied to our bodies hrengh a oe ney are required for proper h T diet ealth and pasetey a6 epee eee growth, meiency of essential amino acids may erase We tes ike Kwashiorkor in which water balance of pays disturbed. eo? i add to Yorn Knowledge {ONFIGURATION OF c-AMINO ACIDS ‘Allocamino acids except elycine are chiral molecules sd exhibit optical activity. Most naturally occurring vonino acids have L-configuration i.e,, NH, group is left hand side as —OH group in L-glyceraldehyde. cHO COOH yo-0-H ea CH,08 R Leralachyde SRUCTURE AND PROPERTIES OF AMINO ACIDS Ithas been found by spectroscopic means that “COOH and NH, groups of amino acids do not exis) ‘sch but they react with each other to form inter Sil structure which is also called zwitter 9% Stueture, In the formation of 2witter 10> paid © COOH part of the molecule is release’ aches itself to —NHL part to consticute 5P 8idlows: Pw kon Lag aba Dwi R « Zaittoy ite ion ‘@-and ion j '8 4 neutral species but carries both Negative charge % aciina aa a ein water lng, They ee moerately 88 cations and eldie solution amino acids exist ficld whereas jrietate towards eathode in an electric nd migrate ton Pasi Solutions they exist as anions Owever, they mals anole. At the intermediate pH, 0 not thigrnte ot 88 2¥itter fon (a dipolar ion) and OWN a8 the gq wat either electrode, This pET is 'soelectrie point of the c-amino acid. ¥sN—Ctt—coon R are usually colourless, OW 7 7 —— Cation R Baier on woo Sets 000 R sin Different amino acids have different isoelectric Points. The isoelectric point of an amino acid depends ‘upon the functional groups present in the amino acid. nates amino acids have isoelectric point in the pH Tange of 5.6-6.3, At isoelectric point the amino acids have least solubility in water. This property of amino acids is exploited in the separation of different a-amino acids obtained by hydrolysis of proteins. a-Amino acids exhibit chemical reactions charac- teristic of primary NH, group and —COOH group. NAMING THE AMINO ACIDS ‘Amino acids are known by their common names. However, they can also be named by following the TUPAC rules. In protein or peptides, the amino acid ‘units are represented by a three letter symbol or a one letter symbol. For example, the abbreviation for glycine and alanine are gly, ala respectively. The names, Structures, and abbreviations of various c-amino acids are given in Table 14. PEPTIDES AND PEPTIDE BOND Peptides are the products formed by the condensation of two or more amino acids through their end carbo groups invalving elimination of ami Scanned with CamScannerFO 820 ified 95 water molecules. They may be classified i dipeptides, tripeptides, tetrapeptides, | depending upon whether the number of amino te molecules taking part in condensation is two, (h7% OF four respectively. When the number of such anit acids is more than ten, the product is cf h polypeptide. The linkage (~CO—NH—) which unites various amino acid units in a pePht! molecule is called peptide linkage or peptide bond. 9 i, sc {OER N—cH-Co0H el HR R Amino acids Condom | 20 = Pentide Bond to H.N—cHLC_NE cHCOOH rid Ri HER ADipeptide Asimple convention is used to write the structure and name of the peptide. The amino acid unit having free NH, group is called N-terminal end whereas the amino acid unit with free —COOH group is called C-terminal end. The structure is written with Neterminal end to the left and C-terminal end to the right. The base name of the peptide is taken from the C-terminal amino acid unit. Other amino acid units are taken to be substituents of this acid and the suffix ine of their name is replaced with y/. In case of polypeptides and proteins, the abbreviated names of amino acid units are used. Let us write the structure of a tripeptide formed from glycine, alanine and serine. o 9° I I H.N—CH.—C—N—CH— C—NH—CH—C_on H CH; CH,OH Gtyyatanyterine GlyAlaSeror 6-4-5 (iano) ASrevated name) A section of polypeptide with different amino acid units is given below: i * ie 1 ~HN—CH—CONH—CH—CONR—CR—co- Polypestize ee | ‘ Sy ‘A polypeptide having molecular mq, " hi 10,000 1 is called protein. hi og CLASSIFICATION OF PROTEINS CLASSIFICATION BASED UPON Moy 5, STRUCTURE Ula Proteins can be classified into two b on the basis of their molecular structure: Fibrous proteins and Globular prote 1. Fibrous proteins. Such proteins hays, like molecules which tend to lie side by side fibres. The molecules are held together at many fey by hydrogen and disulphide bonds. They are. maa insoluble in water. ay Functions of fibrous proteins, proteins serve as the chief structural materialcf ay; tissues. For example, keratin in skin, hai, nails way horn and feathers : collagen in tendons, myosin a muscle, and fibroin in silk. oad lass, 2, Globular proteins. Such proteins kay molecules which are folded into compact units thatefo, approach spheroidal shapes. The areas of costes between the molecules are small. Therefor, tk intermolecular forces, here, are comparatively wa. These proteins are soluble in water or aqueous solutes of acids, bases or salts. Functions of globular proteins. Glob proteins perform diversity of biological functions. Saxe of these are: (a) Some globular proteins function as enzyna which catalyse all biological reactions. Insuis and thyroglobin are some examples. (6) Some globular proteins regulate melatelt Processes. For example, the protein horm* insulin (from pancreas) maintains blood-0 level. (©) Some globular proteins act as antibodies + protect the body from the effect of invadst species and thus, save us from disease. _Some important differences between gti? proteins and fibrous proteins are given in Table 145 Scanned with CamScannerZotinked con polymers 0 ‘ype amine a> aoe slob in wee args solutions of salts folded to give rise mera int ae dimensional sphe- “al share pone ctouin na alee and some hor: enzymes ie 14.3- Differences betw jar and Fibrous Brouing Fibrous Proteins 1, They are li a near ao condens- 2, They are insoluble in common solvents but soluble in strong acidic or| dasie solutions, 3. The Jong linear protein chnins are hela togeth by weenilicdar H-bonds. 4, Examples : fibroin in sill; collagen in tendons ; myosin in muscles e_] (LASSIFICATION BASED UPON THE CORRES- poxDl ature of ‘products of spo three categories: (i) Simple proteins. of a-amino aci siggive mixture etalbumins in white of C88 jinhair, nails, horns and glutenin jin wheat. (ii) Conjugated PFO! hydrolysis give @ non-protel veamino acids. This non-PTON ain function prosthetic group. The ™ ous tocantrol the biolo Some examples of coniugat ssthetic grouPs % corresponding Pro tabular form: Glycoproteins Lipoproteins Phosphoproteins | Chromoproteins Metalloproteins. in part im Y HYDROLYSIS PRODUCTS on the basis of chemical composition or the pydrolysis, proteins are classified ‘These proteins on hydroly- ids only. Some examples ‘oxyzenin in tice, keratin ns, These proteins om addition to the portion is called the yf the prosthetic veal functions ofthe Pro with their re given below in Nueleie ac Sugars Lipids 5 Phosphoric a Some colouring matter such as lecithin jd residues Some metal. in Derived Prot products obtained bY Part pdrotysis of simPlE OF Jugated proteins wil racids, alk ies or enzymes: ‘examples are, Protegsey peptones and Pol ptides. Co proteos | Proteins stones Polypeptides = a2 STRUCTURE OF PROTEINS Th ae structure of proteins is generally studied ot See ere eae ‘eondary, tertigr? quaternary srctures at discused Del " 1, PRIMARY STRUCTURE OF PROTEINS Itrefera to the sequence in which amino acids are es in proteins, Each protein has & specific ae af smino acid units which is critical of its biological activity. The change of just one amino acl in the sequence can alter the biological activity. For example, haemoglobin, is 8 protein responsible fo carrying oxygen in the blood. consists fof 574 amino acid ae, The change of ust one amino ac ip the sequence produces ineffective haemoglobin which is found in the patients suffering from sickle coll anaemia). eae nee Oa ee (Normal haemoglobin) _Val—Hie—Leu—Thr—Pro—¥4 (Sickle cell haemoxlobin ‘The procedure for the determination of primary structure of protein is quite complex. Such procedtre yr in 1953, se firatof all developed BY Frederic Sange? ia sequence in insulin ‘Who determined the amino 2 shown in Fig. 14-2. 2, SECONDARY sTRUCTURE OF PROTEINS Itrefers to Vie arrangerent of pobbepiide SN giving rise to. particular shape, which ‘arises asa result of hydrogen bonding: ‘The two common secondly qchelix and B-pleated ‘sheet structure: (a) Pleated Sheet Structure OF structures are p-Sheet Structure pesheet structure wa proposed by Linus Pauling and co-workers in 195 his type of secondary Seructure, the pepti ” jie side by side in a 218 zag manner W ‘on the same side. ae jeighbouring peptile ‘Ghains are held together PY Vepond, resulting in the formation of intermolecular wre. These sheets are stacked one sheet struct fibroin has Br Scanned with CamScanner_Tnsulin as 51 amino acids arranged in two Poly fone chain has 21 amino acs while the other chain © ‘ye principal source of insulin for medina available. The synthesis of insulin has become lab : has been rl. cys Ser Lae” Gite Vat Gu cn-Cy-CrwAla Ser Vah oe s I »~ testa saw 4 Fig. 14.2. Amino acid H mS a NN H u ° Fig. 14.8, Pleated sheet structure, (6) o-Helix Structure The c-helix model was also proposed by Linus Pauling in 1951. In this type of structure, the peptide chains are coiled up to form a helix (ike spiral staircase ora cork screw). The helical pattern is found to be right- handed and is called a-helix. The reason for righthanded helis is thatall the amino acids in the polypeptide chain have L-configuration and therefore they can result in stable helix only if it is right handed:The H-bonds (intramolecular) are formed between C = O group of one amino acid residue and N—H group of fourth amino acid residue. The achelix is also known as 3.6,, helix because each turn of the helix has approximately 3.6 amino acids and a 13 member ring is formed by hydrogen bonding. The a-helix and H-bonding in a-helix has been shown in Fig. 14.4. Proteins such as myosin in nucleus and keratin in hair, wool, nails have a-helix structures, the pancret sesible by the meth Tye Cys-Asn ayr-Gin-Law-GlerAsnTyr CF Lew.Val-Cys-Gly-Ghi-Arg-Gly -Phe-Phe-TyrThrProys aly ‘sequence in insulin. as of cattle. Nowadays, netic engineering. synthetic insulins, 3 Maley if od of Bet 8 | > Fig. 14.4, a-Helix structure, It may be noted that pleated sheet type structure generally exists in case if R-groups are smaller whereas Ochelix type structure is assumed, if R-groupsare large. 3. TERTIARY STRUCTURE OF PROTEINS Itrefers to the definite geometric pattern in which the entire protein molecule folds up to produce a specific shape. It arises due to folding and superposition o! Various secondary structural elements. The '%? important tertiary structures of proteins are fibrous structure and globular structure. At normal pHs! temperature, each protein will take a shape that 6 energetically most stable. This shape is called natit® Scanned with CamScanner&— tein. Each amino she PTO acid sequer ‘a i eprfate. Tt may be noted ieee has sb Meche tertiary structure depends went? pill! “he between various parts of thot rotein a tio! 8 zh the substit pet stituents present i actions nse rhe following: pa ie or sal bride "agen bonds rer der Waals interaction or \tauphide (S—S) bonds. \PeRNARY STRUCTURE ony proteins exist as aggregate sptde chains. The overall Svcurvat tien mtd Mises due £0 specific spatial crrangeneat of atiple SU units is called quaternary structure. re the quaternary structure of haemoglobin samples n axes four polypeptide chains. 4U DENATURATION OF PROTEINS All proteins in a living system possess definite cwnfiguration and biological activity. protein found ne system with definite configuration and biologica! aah ie ealled a native protein. When a protein ienative form is subjected to physical change such as thange in temperature, addition of solvents miscible with water or chemical: change such as ‘addition of acids, ‘lkalies or salts, the hydrogen bonds are disturbed. AS {result, globules unfold and helix get uncoiled and protein loses its biological activity ‘and gets coagulated. ‘The proteins in this state are said to be denatured. The process bout changes in physical as wel the proteins is called ‘denaturation of proteins. fenaturation are tant features of d iy, denaturation does not hane the atture but changes the secondary structures Of of proteins erature’ Some import (i Chemical primary str cand tertiary 5! (ii) Denaturation changes in pH, temp* denaturating agents. . iy Denatured protein loses its biological activity. in molecule (iv) During denaturation, Y oie from an oraered and ‘specific confor mation intoa more random eonformation ead ing to precipitation. Thus, denaturation leads ie verease in eTtOPY- op ippeversi (@) Denaturation may be reversibleoT irrevers ‘proteins. ‘ean be caused bY ‘or by adding other ible. The mo at cor denaturation of proteins is somrlaton irreversible Present in whit. teins is coagulation of albumin hard the soluble, art of an egg. When the egg is boiled, ay ll lobular protein presenti dena an formation of insoluble fibrous proteins. curdling fA her example of irreversible denaturation is curing of milk which s caused due to formation of ic acid by bacteria present in Natural protein Denatured protein Fig. 14.5. Denaturation of protein. oversible denaturation process, inal properties and biological tive agent is removed. The turation. In ease of r the proteins recovers its origi activity when the disrupt reverse of denaturation is called rena’ a Solved Problems: > Ds Give reasons for the following * rn acidic solution amino acids (i) On electrolysis i ikaline solution these migrate towards cathode while in a migrate towards anode. i) The monoarino monocarboxylic acids have pK values. ‘Solution. () In acidie medium, tions (R- Git COOH atin amino acids exist as ca medium they exist as anions ‘NH (R—CH — COO”). Therefore, onclectrolysis in acidic mediua NHa smigrate towards cathode while in alkaline medium they they wards anode. migrate to i, One pK, value corresponds '0 dissociation of p—cH—COOH and the second value corresponds to 1 “NH ition of B_GH—-COOH NH dissoc Scanned with CamScannerCee eee even bonds or dieuiphize , a jrdrogen bonds or disulp (ats Phide bonay M three amino acide viz. glycine. alanine and phenylalanine react together, how many possible tripeptides can be formed? Write donen the structures and names of each one, Also write their names weing three and one letter abbreviations for each amino acid! Solution. By combination of three different amino acids six different tripeptides are possible. For the given amino acids these are () H.NCH,—CO—NH—CH — CO— NH —CHCOOH 1 | CH,CeHs cn, Glevsialansiphenstalanine GAP H.NCH,—CO-NI—CH —CO—NHt —GuC0oH CHCl, CHs Gloestphenslalanslalanine (Giy-Phe-Ala) GFA ig HCH —CO—NII—CIl,—CO—NH—CHCOOH, CH; CH,CeHs Alanyielyeyiphenslataline (Ala-Gly-Phe) AGA Sed NGL 00SEC CO NH—CH,COOH | CH; CHCl Alanylphenylalanylglyeine (Ala-Phe-Giy) AFG) GE — 00 NE CHl,—CO—NH—CHCOOH CHCcHy Phenylalanylelyeylalanine Phe-Gly-Ala) GA) (ch NCH —CO— NH — Cot —CO—NH—CH,COOH CH, CHyCcHs CH, Phenylalanylalanylelycine (Phe-Ala-Gly) PAG) TREELNEN What type of linkages are responsible for the formation of, ( Primary structure of proteins (ii) Cross linking of polypeptide chains (iii) a-Hetix formation (iv) B-Sheet structure. Solution. (i Primary structure of proteins arises due to peptide bonds (—CO—NH— bonds) between various constituent of amino acids, ” Comprehensive é Siig, | 7 ii) Hydrogen bonds between _¢_ | yo Ww] gh 0 i lo roupe ofthe same polypeptide Gain, 4 (io) Hydrogen bonds between —C— , | yoatmw ie ya belonging odierent peeping | hain ‘NCERT INTEXT QUESTIONS The melting pointe and sntubit Tait acide are generally Maher than that | Corresponding halo acids, Explain. Solution, Amino acids acquire 2witter ion structary presence of both an acidic and a bnsie group in the on vijecule. As a result they behave like crystalline sag, Rave high melting points and high solubility in water onset Wher hand, hale acids cannot form zwitter ion struct hence behave like carboxylic acids od Where does the water present in igo after boiling the eg? acu Solution, On boiling the water soluble globular proteins uxtig ‘and helix get uncoiled. During this change intramolerlee hydrogen bonds get disturbed. The water molecules get attached to the uncoiled protein molecules throurh hydrom |. What is the name given to the linkage that bolis together the amino acid molecules in proteins? 2. Draw structure of alanylelyeine. 3. What is the cause of disease sickle cell anaemia? 4. Give name and structure of optically inactive camino acid. 5, What do you understand by (i Primary structure of proteins Gi Quaternary structure of proteins? 6. Give name and structure of the simplest aminoacid which is optically active. "AWORK OF LAXMI PUBLICATIONS (P) LTD. SS NUCLEIC ACIDS Nucleic acids are long chain polymers that a present in high concentration in the nuclei of cells. Ths play vital vole in the cell replication and pret? synthesis, Nucleic acids are of two types: (i) DNA (Deoxyribonucleic acid) (ii) RNA (Ribonucleic acid). _—_ Scanned with CamScanneric units of nuclei i jpomerie units eic acids a oe Bach nucleotide consat of tiarse sates é it rou? 2 five carbon sugar and a nitro i ff moot base, The mitogen containing 1 He cleotides are derivatives of ete er ji (00 pimidine. Ms yr WA mae aly Wee i iy va i piling Paring primes Purines 0 NH, on, . en’ a N pie Ks oy Wy h ymin ° ey i or 4 sinc outing) wt x pO 4 h pms Bases in Nucleic Acids. The bases derived from purine are adenine (A) ani guanine (G) whereas those derived from pyrimidine arethymine (T), uracil (U) and eytosine (C). The base thymine is found only in nucleotides of DNA and thebase uracil is found only in nucleotides of RNA. The second component of the nucleotides is the sugar molecule. The sugar present in RNA is D-ribose andin DNA is D-2-deoxyribose. _ D.2-deoxyribose differs from D-ribose in not Saving an —OH group on C—2. Ribose 2.Deoxyritore Sugars in nucleic acids: 825 Jhosphoric The bonding between sugar molecule, PI follows: acid ie and nitrogenous base in a nucleotide is a: Zae | Phosphate | ‘nie Sager ‘ OH OH Adenosine Monophosphate. (A nucleotide) Ninety) ‘Nucleoside is formed by condensation of a purine or pyrimidine base with pentose sugar. The bond between the base and the sugar in the nucleoside is known as N-glycoside bond. In nucleosides the carbon atoms of the pentose sugar are numbered as 1’, 2’. 3, etc, in order to distinguish from the numbering in the bases. The purine or pyrimidine bases are linked to ion 1’ of pentose sugar through N-glycoside bond. NH, —— N-Glycoside bond “Adenosine (nucleotide) ‘The nucleotides are expressed in abbreviated form by three capital letters, preceeded by d- in case of deoxy series. For example, Adenosine monophosphate—AMP Deoxyadenosine monophosphate—dAMP ‘Adenosine triphosphate—ATP ‘Adenosine diphosphate—ADP Scanned with CamScanner826 STRUCTURE OF NUCLEIC ACIDS PRIMARY STRUCTURE OF DNA ust as the primary structure of proteins depends fn the sequence of w-amino aide in the protein, the structure of nucleie acid depends on the sequence o nucleotides. The connecting link in proteins is amide linkage while in nucleic acids it is phosphodiester linkage. Phosphate esters link the free hydroxyl at 3—OH of one pentose sugar with the 5'—OH of the other. Thus, nucleic acid is a long unbranched chain with a ‘backbone’ of sugar and phosphate units with heterocyclic bases attached to the chain at regular intervals as shown below: Send of chain ~0-cH, Phosphodiester linkage § send of chain The sequence of nucleotides in a nucleic acid is described by starting from the 5/ end and identifying the bases inthe order of occurrence. Thus, the sequence of bases in a DNA molecule may be indicated in the following way. 5’ aTacr_—,, 3’ Information regarding the nucleotides in the chain of a nucleic primary structure of the nucleic acid, Sequence of acid is called Contre OH Pane) sequence of bases on DNA ig To ant of ON i ge pein, Collection of information resardiy wet dO fingerprinting ix being used these day criminale (iio determine paternity of an individyay ii) to identify the multilated dead bod necident by comparing the DNA's of children (i) to entity racial sr0UupY to rewrite iooge evolution Use of DNA fingerprinting for ident individual has advantage over use of fngerpsan because fingerprints of a person can be altercy surgery whereas DNA fingerprints eannot be ate, by any known treatment. ion of ies in any Parents oy fying an SECONDARY STRUCTURE OF DNA It was observed by E. Chargaff that there cortain regularities in the percentages of bases sin; from the DNA ofa variety of species. He observed that 1. Samples of DNA obtained from species have different heterocyclic bases. different composition of 2. The total mole percentage of purines (A and G) is approximately equal to that of pyrim. idines (C and T), 3. The mole percentage of adenine is equal to that of thymine while that of guanine is nearly equal to that of cytosine. (A+D (C+@) which varies from one species to the other and is characteristic of the DNA of a particular species. This ratio is found to be 1.52 in human beings and 0.93 in E.Coli. On the basis of X-ray diffraction studies, the three dimensional structure (secondary structure) of DNA was Proposed by James D. Watson and Francis H.C. Crick in 1953, According to their Proposed structure, DNA molecule consists of two linear strands of the type shown in Fig. 14.6, which are wound together in the form ofa double helix. The double helix is composed of two right Chargaff observed that it is the ratio _ Scanned with CamScannerS—Sugar P—Phosphate A~Adenine G—Guanine T—Thymine ytosine Fig. 14.6. Double helix structure of DNA, ded helical polynucleotide chains coiled around the oe central axis. The two strands of the double hehe setparalel i, their 58’ phosphodiester linkages ‘ainopposite directions. The bases are inside thes jl sugar phosphate backbone is on the outside. The trochains ofthe double helix are held by y the hydrogen tnnds between the bases on the two chains. The hydrogen bonding between bases of the two stands is highly specific. Thymine (T) pairs with sdenine (A) through two hydrogen bonds and cytosine (Cars with guanine (G) through three hydrogen bonds (Fig 14.7). Corresponding to the structure of these tases, the above combination is energetically most favoured. The other combinations are energetically less feroured and hence do not occur in normal DNA. This mens that the two strands of DNA are complementary to each other. The sequence of bases rene strand automatically fixes the sequence of bases ‘tthe other. Opposite each adenine on one chain there ‘Salvays a thymine on the other chain and opposite ‘Manine, there is cytosine. ‘The exterior width of the double helix is 2 nm. The double helical structure repeats at intervals of Mom. This distance: corresponds to one complete turn ‘2d10 nucleotide pairs. On heating the two strands of DNA separate from rhother. This process is known as melting and the SP Perature at which the two strands separate patletely is known as melting temperature (Tq) of w On cooling, the two strands again hybridize an “Process is known as annealing. be helpful in understanding protein synthesis 2m means by which genetic information is during reproduction of cells. ese go See to has proved The double helix structure of DNA Hs PET ne (a) Thymine NH OG Nawovontt 3 cn S$ Ge HN () Cytosine Fig. 14.7. Hydrogen bonding between complementary base pairs. In secondary structure of RNA, helices are Present which are only single stranded. RNA molecules are of three types and they perform different functions. They are named as messenger RNA (m-RNA), ribosomal RNA (r-RNA) transfer RNA (t-RNA). BIOLOGICAL FUNCTIONS OF NUCLEIC ACIDS . _ Nucleic acids perform two important functions: 1. Replication 2. Protein synthesis, 1. Replication. It is the property of biomo- lecule to synthesise exact copy of itself. DNA has this unique property of duplicating itself. The genetic information for the cell is coded in the form of the sequence of bases adenine (A), thymine (T), guanine (G) and cytosine (C) in the DNA molecules. During division of cell, DNA molecules replicate and produce exact copies of themselves. Each daughter cell has DNA molecules identical to that ofthe parent cell. According to a prominent theory of DNA replication, the two, strands of DNA helix unwind and each strand serves as a template of pattern for the synthesis of a men strand in the cell environment. The specificity of hace pairing ensures the exact duplication of sequence of bases in the reproduced strand of DNA (Fig. 14.8), Scanned with CamScannerthe cell Fig. 14.8. Replication of DNA molecule. 2. Protein Synthesis. The DNA molecules in | nucleus hold the code for the protein synthesis, os Comprehensive SHER ic information is coded in DNA in th, re tuna of haces, The synthesis of vst sotein involves the following two steps. fic a Transcription (ii) Translation Tho transeriptton involves copying of sequen. of bases from the DNA strand on the RNA molecule called messenger RNA (mRNA). The bases. ‘ofthe mRNA, are complementary to thove of the DNA se Messonger RNA contains only four bases adenie 4, suanine () eytosine (Cand uracil U). DNA meet contain the fur bases adenine (guanine Gy eye (Chan thymine (1). The complementary base pane as follows: DNA mRNA ‘Adenine (A) Uracil (U) Guanine (G) Cytosine (c) Cytosine (C) Guanine (G) Thymine (1) Adenine (A) After transcription mRNA moves from the nucleus of the cell toa ribosome in the eytoplasm wha itserves as template forthe protein synthesis Fig 149), maw a88 UGG cac uva cuy mRNA SSO 00E O68 Gon gop Guu ee ee muy AUS UGG’ Gac ua CUU mRNA Translation GUU auaA UGG Gag vf Fig. 14.9. Role of DNA and RNA in protein synthesis, Scanned with CamScannerpases in MRNA are read ina ea roups of three at time. Each triplet of ingen a specific sequence of bases) is ch codon specifies one amino acid. ‘have more than one codons. The ht to the mRNA by another type atjed transfer RNA (RNA), Each amino ie one corresponding tRNA. At comples between, mRNA and tRNA is iit yanother typeof RNA called ribosome RNA. oil ror transfer of ‘amino acid, the tRNA is free speat the process. Thus, proteins with a acksguence of amino acids are produced. The ic #8f'amino acids in proteins is determined by seuence of nucleotide bases on mRNA which in turn sce by the sequence of bases in DNA, molecule. ‘DNA sequence that acts a5 @ code for a specific x4 Sted gene. Every protein in the cell has ram pnding gene. The relationship between the aide triplets and the amino acids iscalled genetic code. The genetic code has four noteworthy features: (i Itis universal. (ii) Itis degenerate. It codons can act as @ (iii) It is commaless. (iv) The third base of the ‘The first two bases of important. ence of ps ol means that more than one ‘code for an amino acid. codon is less specific. f the codon are most xewaledye Pes <<< | Mutations It is a chemical cha’ | nitrogenous bases along |_ nitrogenous peynthests of proteine with altered can lead to the rence. Amutation results due 1.98 samme we a genetic code contained in Dol | tice: this may lead to the synthesis of protrs | ‘Tih new amino acid sequence, Chanke 9 See wrest teute may occur spontaneously or May be 1 ea re ectation, cheraical agent, etc. Changes in DNA are generally repaired by special enzyme tn, the DA tre Reneraure to do so results in mutation. The defective genes can cause abnormalities SERER what are the products obtained on WMA? Write down the names and 2 drolysie of DI siructurcn op porimidine and purine bases present in DNA. ge in the sequence of ‘uith DNA strands that Solved Problems the following Solution. Complete hydrolysis of DNA yields products: (i) Pentose sugar-deaxyribose. (ii) Pyrimidine and purine bases-cyt' adenine and guanine. (ii) Phosphoric acid. osine, thymine, Pyrimidine bases present in DNA are: ° NH, CH, HN” pe 07 1 H Thymine cytosine Purine bases present in DNA are: NH, Guanine Enumerate the structural differences between DNA and RNA. Solution. The main stru RNA, tural differences between DNA and {) In DNA, sugar is deoxyribose while in RNA it is ribose. (i Pyrimidine base thymine is present in. while uracil is present in RNA only (iii) DNA exists as double helix whereas RNA exists as single strand. DNA only tts te ting tempratire Cm) Ca in nor Gobo pat Oe a aT Epi eh stints Sige ore ture at which the two strands of DNA separate io Set canseere known ween temperature (Tm) of DNA. ¥ ‘acne ein wer manent number of GC base pairs than AT base pairs because be con cos C these are three hydrogen bonds a: ene hydrogen bonds between Aan eee gar nd an Ook Scanned with CamScannerCobian 830, ‘NCERT INTEXT QUESTIONS ETSEBEAY When RNA is hydrolyzed there is no relationship among the quantities of four bases obtained unlike DNA? What does this fact indicate about the structure of RNAC Solution. This indicates that RNA does not exist as double strand but exists as single strand. DNA exists as double strand. ‘The sequence of bases on one strand of DNA is complimentary to the sequence of bases on the other strand. Therefore, the quantities of four bases obtained on hydrolysis of DNA have relationship. Since in ease of RNA there is no relationship among the quantities of bases it indicates that RNA exists in the form of single strand and not double strand. What produets would be formed when a nucleotide from DNA containing thymine is hydrolysed? Solution. The products of hydrolysis would be (i) (D)-2-deoxyribose (ii) Thymine (iii) Phosphoric acid (or phosphate). ere) 1. Name the four bases present in RNA molecule. 2. Name the sugar portion present in the nucleotides of DNA molecule. |. Name the base that pairs with adenine in RNA molecule, What is the corresponding base present in DNA molecule? |. What are the two main functions of nucleic acids? . Name the three different types of RNA. AWORK OF LAXMI PUBLICATIONS (P) LTD. —— Gee HORMONES Hormones are the chemical substances which are produced in the ductless glands in the body. They are carried to different parts of the body by the blood stream and control various body functions. The ductless glands which produce hormones are called endocrine glands. Some examples of endocrine glands are the thyroid, the pituitary, the adernals, the pancreas, she testes and the ovaries. The endocrine glands secrete hese hormones directly into the blood stream through vhich they reach different parts of the body. In nammals, the secretion of hormones is controlled by he anterior lobe of the pituitary gland located at the brain. The probable function of hop, ialogical reactions. However, their go tinderstood. Hormones are gga’ i ase of the tocontrol bi is not clearly A is mired to as chemical Messengers boca, transfer information tissue or organ. | | = | | | CLASSIFICATION OF HORMONES | | from one group of cell ta qi? sy On the basis of their chemical constitu hormones are broadly divided into two classes; 1, Steroid hormones. 2. Non-steroid horm, ney, 1. STEROID HORMONES Steroids are the compounds which are deriva of four ring system consisting of three cyclohexane ond one cyclopentane ring as shown in Fig. U1 <0 hormones, bile acids and a number of other biologica ‘active compounds belong to this class. y Steroid hormones can be further classifie: two types : Sex hormones and Adrenocortica} hormones. (a) Sex Hormones. The sex hormones can by divided into three major groups: (@ Male sex hormone or androgen (ii) Female sex hormone or estrogen (iii) Pregnancy hormone or progestine. Testosterone is the major male sex hormone. It is secreted by the testes. It is the hormone that is responsible for the development of secondary male characteristics. The growth of facial and body hair, the deepening of the voice, muscular development, maturation of the male sex organs. Estradiol is the main female sex hormone. Itis secreted by ovaries and promotes the development of the secondary female characteristics that appear atthe onset of puberty. It also participates in the control of the menstrual cycle. Progesterone is the most important pregnancy hormone or progestin. This hormone prepares the uterus for implantation of the fertilized ovum. Progesterone also suppresses ovulation. Many syntheti progestins are used as oral birth control pills. Adrenocortical Hormones or Corticos- teroids. A large number of hormones have been isolated from the adrenal cortex, two of which are cortisone and cortisol. Cortisol is the major hormone synthesized by adrenal cortex in human beings. These hormones are involved in the regulation of large number of biological activities such as carbohydrate, protein and lipid metabolism, water and electrolyte balance, a" inflammatory effect. ion. the tie Scanned with CamScanner<& gxorD HORMONES 1S 1 osteoid omnes donot contain steroid ri further classified as protein or pepti ie a sd derivativ in or peptide hor- papi cid derivative oF amine hormones, ee fr ein OF Peptide Hormones. A well known Pri this tye of hormones is insulin which ix on ‘iby pancreas. Its function is to lower the ‘ood wel by increasing the rate of conversion of 1 Sit elycogen. It deficieney in human beings 5 Fabetes mellitus. Oxytocin and vasopressin rs ‘olypeptide hormones secreted by posterior lobe ‘he ituitary gland. Oxytocin controls the uterine «i Fontraction during child birth. Vasopressin os the reabsorption of water in kidneys. Glucagon, wae by pomereas is also a peptide hormone. Its fation js to increase blood sugar. ae yet HO gstrone 1 HO" T HO s 3. AMINE, HORMONES we meron ce curenaline (epinephrine) are the pa longing to this class. Thyroxin 6 re thyroid and controls the rat of metabolism renaline is produced by adrenal medula. [ts function is reverse of that of insulin, Secretion of adrenaline takes place under the conditions of stress such as fear anger or some other emergency, It stimulates the lycoge-nolysis (breakdown of glycogen) in the liver which given lone The lease thos formed provides the energy necenaney to perform physiolosiea! #77 under stress, Structure of some of the important hormones 2F2 given in Fig. 14.10. cu, Progesterone on cul 0 ‘Testosterone CH OHH Na zo Adrenaline 1 —cu-COO” 0 ic CHy | NH, 1 Fig. 14.10. Structures of some ‘Thyroxin hormones. Scanned with CamScanneree EY = .s are listed in Table 14.4. » yn of some hormones 5 ‘The source, chemical nature and funetio ‘Table 14.4. Some TyPica 1 Hormones Function Soare | Chemical a Hormone = sa | =o acid | Stimulates metabolism. | nae ene Tnerenses pulse rate and blood pressure, | 2 Airenaline Adrenal | Amine releases glucose from glycogen pens nd fatty acids from fats. sases blood glucose. | Peptide | Deere 8. Insulin Panereas ten 4. Glucagon. Pancreas | Poptide | Increases blood ah et Testes | Steroid Controls normal functioning of male | 5. Testosterone es Controls i smal functioning of female Estradiol | Ovaries | Steroid Controls nor! : 6. Estrone and Estradiol | 0 comes | i 1s uterus for pregnancy, controls rogesterone Ovaries | Steroid Prepares ut “ieee menstrural cycle. 8, Cortisone Adrenal | Steroid Metabolism of water, mineral salts, fats, : cortex proteins and carbohydrates. 1. Name any two endocrine glands in our body. 2. Give examples of two steroid hormones and two non: steroid hormones. 3. Name two hormones which are produced by pancreas. 4, Name the gland which produces progesterone. 5. Name the hormone which contains iodine. What is, the function of this hormone? AWORK OF LAXMI PUBLICATIONS (P) LTD. ae VITAMINS The organic compounds other than carbohydrates, proteins and fats that are necessary to maintain normal health, growth and nutrition are called vitamins. It may be noted that vitamins are not used in building cells or as an energy source but they act as catalyst in biological processes, their deficiency causes serious diseases. cal cw oh, \ . ei bb be exon NAN PN Ne | I h h h h = Vitamin A HO oH CH,OH no Lion a 7 cxvo1n cx,08 j R " ne? Sw Vann € Wins (Ascorbic acid) (Pyridoxine) ‘The vitamins are complex organic molecules, however, for the sake of simplicity, they are represented by letters such as A, B, C, D, E, H, K. Plants can synthesize all vitamins. However, human beings and other animals can synthesize only # few vitamins. Human body can synthesize vitamin A from carotene. Some vitamins of B-complex family vitamin K are synthesized by microorganisms preset in the intestinal tract. Vitamin D is produced in UF Scanned with CamScanner«te hat pM cxT1ON OF VITAMINS mins are broadly classified i ye vitamins and fat solu sip. band Karefat soluble wherens vt Je Naior soluble, Vitamin H @iotinyienern es Ca nor im water. Fat soluble vit 8 neither en and adipose tissues, Fat soluble’ culete inthe body. Therefor, excess arn 88 intake ruins may cause by pgs yPervitaminoses, cl into two t pes ble vitamins, Table 14.5, 833 Water ; much jenee lUble vitamins are stored in the eolls in eens te, metnt. Hf these vitamins are taken in © are removed through urine. Water soluble vitami ‘ ins must be supplied regularly in diet. DISEASES CAUSED RY DEPICIE! ' a ‘AUSED BY DEFICIENCY OF Dofici fiona Ney of ome or more vitamins leads to a avtta gam in human beings. This is known 1osis, The various vitamins along with their sources and the a ir deficienei Viti ‘mins and Their Important Sources Chemical Nature i Important Sources Deficiency Diseases Vitamin A, Carotenoids. Soluble in oils and fats, but insoluble in water. It is essential for growth, and vision. etables, Milk, butter, Tver ol caste 2a ith, cod Night blindness, xerophthalmia (cornea becomes opante) dyin of skin. al te yellow veg. itamin B,, Thiamine. Soluble Unpolished Hi jnwater, destroyed by heat, tirarreoteeed tables and fruits, yeast, liver, milk, green vege- whole cereals, | Beri beri, loss of appetite Vitamin B,, Riboflavin. Soluble | Egg white, live Witsater. Stable to heat, de- ane milk, green | Cracked lips, sore tongue and skin stroved by light, : disorders. Vitamin By Pyridoxine, Cereals, milk, egg yolk, yeas, | Nervous disturbances and conval- liver, legumes. sions. Vitamin B,, or Cyano cobala- min, Soluble in water and con- tains also cobalt, red crystalline. | and curd. Present in all animal tissues. Present in liver, kidney, eggs, Pernicious anaemia (RBC defi- cient in haemoglobin). Vitamin C, Ascorbic acid, C,H.0¢, Soluble in water, de- stroyed by cooking and exposure to air. Maintains healthy skin andhelps in development of body resistance against diseases. ‘Oranges, lemons, grapes, toma- toes, eabbage, leafy green vegeta bles, sprouted seeds. ‘Scurvy, dental caries, pyorrhea, anaemia. Tafantile rickets; Osteomalacia. | Vitamin D, mixture of 4 complex compounds containing C, H and) 0. Soluble in fats and oils but in- | soluble in water. Stable towards heat and oxidation. This vitamin} regulates the absorption of cal- cium and phosphate in intestin®- Vitamin E, Tocopherrol. Mixture ‘of 3 complex substances contain- ing C, Hand O. ‘Soluble in fats and oils but insoluble in water. Stable) Vitamin K, mixture of to 5 plex substances containing Gis | and O, Soluble in! fats but inso” ble in water. Stable to heat an¢ oxidation. other fish-liver catalyse the vitamin D inside oil, germ. Cod iver oil, Halibut liver oiland Called (eunshine vitamin). ‘halk, ghee, cottonse ppeant oil e#8 ¥0l oils, Sun rays formation of| the skin, hence [oss of sexual power of reproduc- tion and muscular weakness. red il, cor Ik, wheat> Tendency to haemorrhage and jmpaired clotting of blood. a —— Scanned with CamScannerNATAL =FTS eT a) Vitamins are organic compounds which are essential for maintenance of normal growth and health of the organism, Certain vitamins cannot be stored in our body and have to be supplied regularly in diet while others can be stored in the body. Vitamins are required only in small amounts and should not be taken in excess. Answer the following questions: (0 Out of water soluble and fat soluble vitamins which can be stored in our body? (i) Name any two water soluble and two fat soluble vitamins. (iii). Which of the vitamin belonging to B-complex series ‘can be stored in our body? (iv) Name the diseases caused by the deficiency of following vitamins: (@) Vitamin A (®) Vitamin D Name any two water soluble and two fat cog vitamins. be , Name any two vitamins which are synthesized * in human body. Explain why fat soluble vitamins should not by taken in excess. } Name the deficiency diseases caused by deficiency (@ vitamin A (ii) vitamin B,, (v) vitamin D. . Why vitamin C cannot be stored in our body? (NCERT Intext Question) |. Name the vitamin whose deficiency in our body results in impaired clotting of blood. (id vitamin B, (iv) vitamin C "A WORK OF LAXMI PUBLICATIONS (P) LTD. See Scanned with CamScanner~ monosaccharides? are sharides are simple \onosaccharides ae simple cnrbobyitrates jan tpaysed t0 still simpler earbohydrerae Spm ase and HUtose, 8. For ’ re ane redoing SWEATS? 2m Te carbohydrates which ean reduce Totten’ {ot tiingclution ate lssifed as educingeuens ete, glucose and fructose are red is icing sugars (cea ears contain free aldehyde or keto ee vs ke se fameth ie group, wre evo main junctions of carbohydrates j on Hint. See text, Section—14.6, Importance of Sites AP cuss the following into monosaccharides and Joccharid sen ibose. 2-deoxyribose, maltose, galactose, fruc- cand lactose. i “Sruon. Ribose, 2-deoxyribose, galactose and fructose are Soncctharides. Jee and lactose are disaccharides. us What do you understand by the term glycosidic linkage? ‘cltion, In oligosaccharides and polysaccharides, the two ‘asaccharide units are linked together by an oxide or ether {nlage formed by the loss of a water molecule. Such a linkage lwimeen two monosaccharide units through oxygen atom is cled glycosidic linkage. 186. What is glycogen? How is it different from. starch? Sclution. The carbohydrates are stored in animal body as Aropen. It is also known as animal starch. Its structure is salar to amylopectin and is rather more highly branched vheras starch consists of two components-amylose which is liner polymer of c-D-glucose and amylopectin which is ‘tanched polymer of a-D-glucose. 144. What are the hydrolysis products of (a) sucro and (b) lactose? d Solution. Hydrolysis produets of sucrose are o-D-glucose ot EDiractoe wioean hydrolysis products of lactose 87° Dgalactose and B-D-ghucose. 18. What is the basic structural difference betw March and cellulose? Slution, Both starch and cellulose contain dares ee D(4) glucose units. Starch consists of = con porta (9 amylose whieh is a linear polymer and ©) 835 which is ah Ae inked re Polymer hut in both the Deuce units ‘ugh c-glycosidic linkage between (of ane elt Cot ment glucose unite : Cellulose ig joined ¢ytlos is only a finear polymer of D-glucose units through B-glycosidie hy eosidic Linkage between C, of one glucose with Oyo nenticore unit nn meen Coton 14.9. What Fag at happens when Duzlucone is treated with the following reagents? amt (i Bromine water (i) HNO, Solut on. Hint, See Section—14.3. 14.10, Enumerate the reactions of D-glucose which cannot be explained by its open chain structure, Solution. Hint. See under the heading ‘Cyelie structure of slucose’ in Section—14.3, 14.11. What are essential and non-essen acids ? Give two examples of each type. Solution. Out of20 amino acids which are required for protein synthesis, the human body ean synthesize 10. The amino acids which the body can synthesise are called non-essential amino acids. The remaining 10 amino acids which the body is not able to synthesise are called essential amino acids. Leuicine and isoleucine are essential amino acid. Glycine and alanine are non-essential amino acids. 14.12, Define the following as related to proteins: (@) peptide linkage Gi) denaturation. Solution. Hint. See text. {The likage (~CO—NH) which unites various ming acid units in a peptide molecule is ealled peptide linkage. (i) See Section 148 Gi See Section 14.0. ust. What are the common types of secondary strucs tures of proteins tem Hint. 1- Pleated sheet structure or Bheet struc Solutio th puget chains are uly extended Kinearly in space pel structure in which the polypeptide chains arocoiledup fora boix‘The hela patterns found tobe aregr handed and ie called acl (i) primary structure Scanned with CamScanner14.14. What type of bonding helps in stabilising the achelix structure of proteins? Solution. There is intramolecular H-bonding betseeen ~ NU up of each amino acid residue with YC=0 of an adjacent eroup ‘h d resid ith YC =O of an adj turn of the helix, 14.15. Differentiate between globular and fibrous pro- teins. Solution. Hint, See Table 14.3 14.16. How do you explain the amphoteric hehaviour of amino acids? Solution. Amino acids are amphoteric because they enn accept as well as donate a proton, 10! aster? nat-ent-coon +H,0 u—eat-—co6 —| i . Loi» H.N—CH—COO + 1,0 Tory ¢ Amie wid in sete on fr I 14.17. What are enzymes? Solution. Enzymes are naturally occuring simple or conjugate proteins which act as catalysts in the biochemical reactions in living organisms. 14.18, Whi of protein: Solution. Chemically, denaturation changes the secondary and tertiary structure of proteins but does not bring change in its primary structure. The denatured protein loses its biological activity. For example, on boiling egg, the soluble form of globular proteins undergo coagulation to give fibrous proteins which are insoluble in water. 14.19. How are vitamins classified? Name the vitamin responsible for the coagulation of blood. Solution. Hint. See Section—14,14, Vitamin Kis responsible for coagulation of blood and its deficiency causes impaired clotting of blood. 14.20. Why are vitamin A and vitamin C essential to us? Give their important sources. Solution. Hint. See Table 14.4. 14.21. What are nucleic acids? Mention their two im- portant functions. Solution. Hint. See Sections—14.11 and 14.12, 14.22, What is the difference between a nucleoside and a nucleotide? Solution. Nucleoside is formed by condensation of a purine or pyrimidine base with pentose sugar at position 1. When nucleoside is linked to phosphoric acid at 5’ position of sugar moiety, we get a nucleotide. So a nucleotide has three units: phosphate group, pentose sugar and a base and a nucleoside has two units: pentose sugar and a base. is effect of denaturation on the structure = CSS, Ho-1,c H H on On ° i Of 0-H oN te of i Ci " Vi on On Oya mcerite 14.23, The two strands in DNA are not identi complimentary. Explain. Solution, DNA is a double helix in which the two strands ot DNA are held by the hydrogen bonds between the bases oq the two strands. Thymine (T) pairs with adenine through tay hydrogen bonds and cytosine (C) pairs with guanine () through three hydrogen bonds. So opposite each adenine (A) on one strand there is always a thymine on the other strand and opposite euanine, there is cytosine. This means that the two strands of DNAare complementary to each other. 14.24. Write the important structural and functional differences between DNA and RNA. Solution. The main structural differences between DNA and RNA are: (0 In DNA, sugar is deoxyribose while in RNA itis ribose. (i) Pyrimidine base thymine is present in DNA only while uracil is present in RNA only. (iii) DNA exists as double strand helix where as RNA exists as a single strand, Functional difference between DNA and RNAs that DNA has the property of replication. DNA controls the trans mission of hereditary characters. On the other hand, RNA controls the synthesis of proteins. : 14.25, What are different types of RNA found in theell? Solution. There are three types of RNA in the cell. These "> (@ messenger RNA (mRNA), (if) ribosomal RNA (rRNA) and (iii) transfer RNA (RNA). —aa—— | Scanned with CamScannerSof Ived Questions ’ Trvol High ee igher Order Thinking Skills (HoTs) reactions of glucose whi pie erpain structure? 7 1e of the presence of an ald f eh sy gest the pink colour of Schiff's i a Heron products with sodium bsulpite ae an Fried 1. Js orm ies acetate does not re , cose penta es ycose Ps not react with hydroxyl 4, aucose eenting the absence of aldehyde group, aus ee hydrogen chloride gasi Nypen ry bydrogen chloride gasis passed s.Whtove in methyl aleohol, a reaction Sie pear of methyl O-D-slucosie and ‘methyl BD. 1 formed: These elucoides donot reduce Febling’s pet alo donot react with HON and hydroxylamine. ei icates that lucosides do not have free—CHO group. rng te formation of gluosides only one molecule aptteombines with a molecule of glucose. rte dour the structure and names of the products | BB ote D-glucose treated with i (i acetic anhydride (i) bromine HNOs. (ii cone. on. () With acetic anhydride: | sti | quo | (CHOH), + 5(CH,CO),0 \ CH,OH a CHO | (CHOCOCH), + 5CH,COOH \ CH,OCOCHs Penta acetylglueos® (i) With bromine: CHO coow o | 2, (CHO Br B, (CHO), +|0| ae | ld oxidizing | CH,OH 837 (ii) With cone. HNO, otto cooH uno, | ( oxo, +3)0] — (CHOW, CH,OH a ; eet (saceharie acid) HERR What are th are the hydrolysis product of sucro BO te tt arc oe Solution. Hort CiaHag0y; ——> CaltisO6 + Colin ceDeglucnse pD-fructose HO/H* CgH20y ——> Opts + CaFli2Os Tactoe Galadose Glucree Sucrose 01 CygH,0y,; ———> 20H 1205 - altace a-D-glacase HEIR Drow open chain structure ofthe following: (@ an aldopentose (ii) an aldohexose (iii) a hetohexose. Solution. CHO guso# geo los (7° H-G-OH = HO-G-H jo—f-OH I y-¢-oH |= H-t-0H «HF 08 H-G-on Hf OH (0H HOH CH,OH CH,OH i ‘alucose Fructose attapentos)—(dabexoH=) (Ketohexose) ld you convert glucose into heptanoic acid? (q) How wor of sodium hydroxide on glucose? (@) What inthe effet Scanned with CamScannerLott ono ence coon dhiow, 2% daca, Meets gor. tion non non rm ano cnyeny,coont ‘Hn wo th When eluewsr te heated with concentrated ction of eyes tint irae glow hem Brome” td Finally tsiniine iv When phicone ie trented with dilute sodticrm soivn it undereoes » reversible iectmeriration yin enultine i the formation af a mixture of Dien, D-fructose sand Damannoee ‘Thin renetion is known ae Lobry de Bruyn van stein rearrangement D.Ghucos == D-Mannoce == D-Fructose It t= beentse of this isomerization that D-fructose reduces Tollen's rwagent and Fehling’s solution in alkaline sxexinii although it does contain any aldehyde group. Phe MBE 1 ire amino ovids vic. glycine, alanine and phenyl Yanine react together, how many tripeptides are possible? Caine three letter symbol of theamino acide rite their names. Solution, Sis tripeptides are possible. These are (0 Gly-Ala-Phe (i Gly-Phe-Ala (ii) Ala-Gly-Phe (iv) Ala-Phe-Gly (0) Phe-Gly-Ala (0) Phe-Ala-Gly. MEE Wr are peptides? How are they classified? What is peptide bond? Solution. Peptides are the products formed by the condensation of two or more amino acids through their amino and carboxylic groups involving elimination of water molecules. They may be classified as dipeptides, tripeptides and polypeptides, depending upon whether the number of smino acid molecules taking part in condensation is two, three ‘or more than three respectively. The linkage (~CO—NH—) which unites various amino acid units in a peptide molecule 48 called peptide linkage or peptide bond. o I Baer (On + Hi) y—eHtcoon ik Hk Amino acids Condense, HANH CHt—cOOH Ri HR Boe " Merve protein) DYMaLUPaign maturation ca Re . sancan 1 Native protell 8 he Drosin fy, Sotutiar Aofinite configuratio ia stony it mad big 8 rototeal i mun. subjected ‘an When « pratain 48 aubyocted 20 some yh ly neat evanrsont wie SEUEN i Kihei cesta denaturation. 1 fetivity, For examen se reenshle ar inrewnesihl Gi Rematueation. fn many 240% a denateyd yy recovers te phssieal an chemical propertion and gg reer en the disruptive enti removed, Tig ptt Shieh ie reverse of denaturation, i knovn a nature sivetine ita primary atruetire, the peoenay jt ue ematared protein loves iy yolk 6, hotline af an ett, The denatiyys many What arr essential and nonessential aminn ari, ico example of each. a fon. The amino acids which cannot be Rete naieed he supped throu our deter nean! teseential amino acids. There ace about 10 essential ass eid. For example, valine, leucine and lysine, “The amino acids which can be synthesized in the body are known as non-essential amino acids. There 2. about 10 non-essential amino acids. For example, given, alanine, serine. LB Name the following: (i An a-amino acid which is not optically active. (ii) Pyrimidine bases present in RNA. (iii) Disease caused by deficiency of enzyme pherst alanine hydroxylase. (iv) The secondary structures of proteins. (v) The sweetest carbohydrate. (i) A reducing sugar and a non-reducing sugar Solution. ( Glycine (ii) Cytosine and uracil (iii) Phenyl ketone urea (Gv) ccHelis and B-sheet structures (©) Fructose (vi) Glucose is a reducing sugar while sucrose is aman reducing sugar. MIRE Draw the structures of the following tripeptider © Gleylatanylphenylalanine (ii) Alanylglyeylphenylalanine Gi) Phenylatanytglyeylatanine Solution, “ pelea ott H CONE Ha CH,CeHs, = CH, a | Scanned with CamScannercH.—Co_NH. "HCOOH cit -00— Nii-CH,cO_w_ ne /H. cis cH,CeHs a7 cn, pjea nucleoside? Write dow wich is present only in RNA. _aenn v4 pe N-yeosides of purine or pyrimi pyri nears are known as niucleosides. ine seats pace + Sugar === Nucleoside se pentose sugar present in RNA is 1 i oe is ribose while in The nucleoside formed by combination of il son iepresent ony in RNA, fon of ec and 9 NH ° A, HOH, on on What are the products: obtained on complete hydrolysis MIDNA? Write down the structures “and names of pyrimidine sd purine bases present in DNA. Solution, ean yarayssot DSA ee deoxyribose, heterocyelic nittoy yaccs-thymine, cytosine, Adenine ana guanine, and phosphors acid. "The pyrimidine bases DresenED [DNA re thymine and ‘xtonine while purine bases present? [DNA are adenine and — ° NH, CHy ne N HN N pa) cr u ih —_ = . Nz ; ie) IW oy : " Guanine G) Draw the structures ofthe following: ir A ‘Sugars present in nucleic acids. Solution. (0S . Ais ribose while in n() Sugar present in RNA ile in DNA is HOH,C Sugars in Nucleic acids (i Adenosine monophosphate NH, N. SN / CA ol NTN tase — We o-F-OF MH, Za oO { ~~ HW sugar Phosphate Ce Unit on OH ‘Adenosine monophosphate wnat ia miteotdet Ge fll form of AMP ond upp. Solution, Neleotides are the monn YO of nucleic acids {RNA and DNA). A nucleotide is * phosphate ester of (RAN de A neloaide consists of PURE Tt pyrimidine nucleo consists of 0 pine of 8 YTiMiAE base, a five sat pugar and one oF mre phosphate FTN Base + Sugar + Phosphate AMP stands for deosy adenosine ‘monophosphate and [UDP stanuls for uridine diphosphate jucleotide What are complimentary bases? Draw ructir show Hydrogen bonding beter vetpnine and thymine and beter sivanine and extosine i rn bonding between bases of the 16) Soft of DNA is highly spect ‘Thymine (T) pairs with ‘adenine (A) throurh iy popenbonds andcytoine (©) Bre adenimyanine (C) sbrouds three bairve bonds, the above Titpination is enerseticaly 02) favoured. The other compination and ence do wok oct normal DNA. Then complimentarybaseofadenine SU while ene, The hydrogen bonuding between that of guanine is cyto ‘Menine and thymine and cytosine ‘and guanine is shown in next page: Scanned with CamScanner“Anawer the following abOUt Protein synth nH a wal’ i do THYMINE:ADENINE i A w—Htemnd) ON, ¢ n sti 9 a aN sat yen co evrosine:ssGUANINE What is replication? What is the mechanism of eplica- tion of DNA? Hote is this process responsible for preservation of heredity? Solution. Replication is the property of biomolecule to synthesis exact copy of itself: DNA has this unique property of duplicating itself. During division of cell, DNA molecules replicate and produce exact copies of themselves. Each daughter cell has DNA molecules identical to that of the parent cell. According toa prominent theory of DNA replication, the two strands of DNA helix unwind and each strand serves as a template of pattern for the synthesis of a new strand in the cell environment. The specificity of base pairing ensures the exact Guplication of sequence of bases in the reproduced strand of DNA. Since due to replication each daughter cell has DNA molecules with exactly the same sequence of DNA molecules ‘with exactly the same sequence of bases as in the DNA of the parent cell, this process is responsible for preservation heredity. reame the facation Where Protin eyes iB Miao 64 codons code for only 29, pe oy, station Potensthess takes placeon yee imieestonnem : = i) Fora particular amino acid more a i aa, sony pre, CU and CUC act as codon forewing fer potine GCC, CCA, CCG, and CCU acts agendge eh, Comment briefly on the chemical nature of is phyaoogieatity Finan ang Solution. Insulin is @ polypeptide hormone seq pancreas. ae Tete by Its function is to lower blood glucose level the rate of conversion of glucose into glycogen, byincraiay It facilitates entry of glucose and other sugars ing, cells by increasing penetration of cell membra augmenting phosphorylation of glucose. This decrea ‘concentration in blood and because of this insulins known as hypoglycemic factor. Insulin promotes aati processes and inhibits catabolic ones. Its deficiency inte, beings causes diabetes mellitus. (a) Name of the following: (@ Awater soluble vitamin. (i An oil soluble vitamin. (iii) A vitamin which is neither soluble in water rr fat. (iv) The disease caused by deficiency of vitamin B. () The diseases caused by deficiency of vitamin C. (b) What do you understand by avitaminosis? Solution. (a) () Vitamin (i Vitamin D (iid Vitamin (iv) Beri beri ( Scurry (6) Avitaminosis is the conditions caused by lackefsat than one vitamins in the human beings. I ang se Scanned with CamScanner844 Summary Biomolecules are the complex or hich build up living organisms an YT life. Carbohydrates, proteins, enzymes, vitamins, of biomolecules. ‘Banic molecules id form the basis nucleic acid ete., are some common examples Carbohydrates are optically active pol 01 sichydes or ketones or melecules amen ee units on hydrolysis. They are broadly classified into three groups—monosaccharides, disaccharides and polysacchardies. Glucose and fructose are monosaccharides; sucrose, lactose and maltose are disaccharides; starch, cellulose and glycogen are polysaccharides. Glucose, the most important source of energy for mammals, is obtained by the digestion of starch. Monosaccharides are held together by glycosidic linkages to form disaccharides or polysaccharides. Proteins are the polymers of a-amino acids. There are about 20 c-amino acids which have been identified as the constituents of most of the animal and plant proteins. Ten amino acids are called essential amino acids because they cannot be synthesised by our body, hence must be provided through diet. Various amino acids are held together in polypeptide or protein molecule by peptide linakge. Proteins perform various structural and dynamic functions in the organisms, Proteins which contain only c-amino acids are called simple proteins, The secon z mdary or tertia structure of proteins got disturbed onchange of pL oF temperature and they are not able to perform their biochemical functions. This is. called denaturation of Proteins, Nucleic acids are the polymers of nucleotides which in turn consist ofa base, a pentose sugar and phosphate unit. There are two types of nueleie ncids—DNA and RNA. DNA contains a five carbon sugar molecule called 2-deoxyribose whereas RNA contains ribose. Both DNA and RNA contain adenine, quanine and ‘cytosine. The fourth base is thymine in DNA and uracil in RNA. Thymine, uracil and cytosine are the heterocyclic basis derived from pyrimidine while adenine and guanine are derived from purine. The structure of DNAs a double strand whereas RNA is a single strand molecule. DNA is the chemical basis of heredity and has the coded message for synthesis of proteins in the cell. There are three types of RNA— mRNA, rRNA and tRNA. Vitamins are the organic compounds other than carbohydrates, proteins and fats that are necessary to maintain normal health, growth and nutrition. They are classified as fat soluble (A, D, E and K) and water soluble (B group and C). Deficiency of vitamins leads to many diseases, Fat soluble vitamins, if taken inexeess, get stored in our body. On the other hand, water soluble vitamins if taken in excess are excreted through urine, Scanned with CamScanner