atrodution LWhat do Bislegists de 2 Ecosystem + Population | individual Organic system Disestive systern)) Organ (Stomach) v | _ Tissue ( Smooth muscle) | 4 : | Cell — (Smooth muscle cell ) vr : Orgonelle (mitrchondira ) v 5 Macromolecute { Protein) ¥ Monomer (Amino acid ) v Atoms { Carbon’) | Figure’ 12. Levels of biological erganisation from atoms , the smallest _ Fe components of Iiving things, to the biosphere , the entive living olanet{Biclogists study every aspect of life at every level of ues organigations ‘om Hie atom that achually make up the molecules tone. biosphere «ecosystem that maxe up the biosphere Why do we study Cells 2 + =! ° Alioughs living things may vary in appearance and size,all_are composed 3 Jena of the loasic touilding bolecks called Cells st plest unit o£ living matter that <: \Scme of the simplest organisms such as bacteria, algae consist of 4 single. cell. In contrast, the human body is made of trillfonsef cells ive processes. of such complex _organigms clepend on the coordinated Sedium_ ig made of only one kind of sodium atoms. So, it ig an element ac kon ercury are algo elements living,dead none-Living Hung 4 are made. of element: Only 21 s¢ the 42 aaturally occuring elements am essential for life. Abe most common elements in organisms are. i). These ae the must important et ents *b life. Other elements eccur in living erganisms. in smaller quantities ; these include ghesphoras (P) peiassium (Kx) sodium (Ni , as owalent bonding) results. in filled eutormost sell. ie is a sheng fore of attraction hiding thartogether, This force is called he Covalent Bend. Covalent bend_is 482 shongect chemical bend, I bo chans are shared betueen atoms fp form molecule Most atoms use this tude o¢ bond when they come together. Tt perms a. ston 4 and stable link between thems we hydreqon atoms alpne have ene electron in a 1 erbital There mare 40 ype8 of covalent: bende namely: Non pular and Polar valent bondsjon-sblar covalent bonds Coiglent bends that are formed between identica\ atoms: as in (ea) oy dh diegen gas (Ha) are the strongest because thelr electrons are lly! shared. Stace the electrens are equally distributed between therhio Se molecules are saiel 4p be Nona ee Hydrogen and Metiane) lar vt hoo es stun dlggorent atoms hoveer the e be pulled truards one atom ‘han the other. The side of the cule, towards’ which the electrons are pulled is electrically negative in comparisen odie ether end. Such a malecule is caid +e be polar (ire tt hos. Ja. positive ant a. negative form). Moms of oni gen, aitregen and phosphorus “Birongly attract electrons and therefore are called Electoneqative ortoms uthen wrt, othor atoms Water ‘is the most abundant miecule in the brody and. here ‘it sonves aS 4he Layer of water molecules ~ with €= ends pointing towards the positive ten. Non polar substances suchas cil have no charge on their mol do not dissolve in water and are therefore called Hyslrophobic3.1 Water is a liquid af cone temperature . le with molecules a6 small as 4. are usual ops) temperatue. Water if a Liquid af nt. 0 Vsendiing: One a0 molecule. can bonds wits up to four othe Ha) molecules. sempecatuce. HaS is a gas af reom temperature, Th re i a Ss action between its pretons. 2 _ electron: the hydreqen-atems “Therefore, it forms ne hydrogen, ond hence ib ik 0. gas at room temperature | a Tatar hae igh mating and bing substance lela mobi) [ome ae a | Water (1.0), 12 o 100° tot’ _| Liquid. Hydrogen Sulphice ae = 85% -6" Ere Gas CD) Ammonia (Nig) | 1% —38 -33 2 ee ‘Methane (CH) 16 = 132° = 16e 12 Gos Coron Monoxide | 28 = 144° Palas 1g Gas (co)melts at Bc a boils at 160° These oe very unssual. melting 2 made Tee small_molecutes wiOUS pai ind beilin, of Bsr made up of molecules that are of a similar size to wate « [sean be seen trom Ate dable., ie sulastances sift sould ca at Oc So none o| vould Se fore iol logical lcci h iceman and_b-p 1s that there ave. cons forces of attractien between the melecules. “These attractions axe hydrogen bonds ete attraction 0 He: meleculas melt and is need wercome pie sea ee aa aa thus allowing the mdecules te move ie 9as_er_vico—versa.. Water also remains _ ature @ much larger range than any lothar cubstance made 4m such small molecules. The forces of attraction between -Hla melecules of ie H.0_ ave ver shong - So, fo (ot of energy is. overcome fem and molecules a form a. gas. zi eas «| Water and Temperature15.1 Specigic heat capacity of water Tp energy is. supplied “fe o. substance the molecules will have-mure Kinetic: energy, and the temperahire op the substance will cise. In liquid HO some of Re energy ques Int breaking fe hydrogen ben, | Atha mole Bir ether, sand daly part. into _ increasing the 4empersture.o quid. This i uhy tb requires a. lot Lenacay ie yale ie temperature of Lea gk. ater ey ce tle be ois in/oaneae eee nds. The quantity of heat in calories required to rise the temperatures of Tatu Auough Picea) Substance Specific Heat (calories) Water 1.00 Ethyl alcohol (Ethanol) 0.6 Sugar (Sucrese) 0-8 Iron Ort Satt_(Nact) Oat [one Calery is degined os fe emeunt of feabndfat uill mise He ure s§ One gram of water by 4° tw specific an alechol, Sgn in the. “able aod it is approximately 0.5 calories wail raise the, temperature of 1g of an atechol by 1°C. Tk is ten times that of Ln The ia specipic heat of water is a conseq hydrogen bendis Helos in water tend to restrict the movement of +e melecules in erder rte kinetic. os 4 ‘increase sufficie . empocetwre_ to oise_by PC ‘i 6 necessary girs fp brea & qumber fie it luonds (alding ie molecules trgetfer: |[What does the high speci gic heat of wader mean in biological terms ? Te means thot the temperature of wetter will rise more sleulythan the temperature of almest any ether material. In contrast, the temperature {ull rap mote stously as heat is removed. As a wsult, oxqanisms that live in-eceans or-large bodies. of frash water Live in an in eaviveoment ae of weer is relatively constant. [5.2 Yapia aaitanaes Wades a high latent heat of waperisadien. A lot of heat energy is needed tp evaporate water. When wader evaporates froma Surface, ik draws heat energy out of the material underneath creating. a cooling efgect Yaper'zation oe evaporation is the. change ‘sion a a quid > aos. Warter_ has q high heat of vaporization . el Phe Adlite hele ie chute thencod aad bie claceieaer em wey nfl ale |(Ahe quantity of heat in calories required te convert 1 gram of liquid te [4 gram_of gas) | Liguid Heat required (in calories), Water ak O'C iss 546 Water at 100°C 2 540 Ammonia 3d 5 Ether etAt water's boiling point it taxes 540 calories to change ene. gran of Ligui water inte vapeur, almest 60 times as for ether and twice as much as for ammonia » Hydrogen bending is alee responsible for usrter’s “high heat of vaporization . Te order fer a wseter mole: +e break frum its fellow molecules, the Hb have to be broken. “This equines heat enerqy + As a. consequence, when wcter {evcporetes. as -fotn fie Surface ef spur iin.or leae of plant the escaging cy a arent deal of heat aumy with them. “Thus , eva; thas a steoling “eppect - j Seaport Fan ‘the surface of a plant or animal ic one of the principl | these organisms hos evslved a mechanism or lowering the bad Aemperature. For example sweating in mammats | 6. | Density and Freezing Properties of Water | Weight = Nelume x Denstty 10 qams = 10 x (for liquid ) 10 grams = 20. ¥ 0.5 -( fr ice) oh the amount of bonding betwen 420 metecules AL BC, dhe freori ing paint of uater, the meleculas are atranged. ino {dita “hexagonal. “crystalline. neturk in which each water motecute is lhydregen-beoded ts four ethers. Mt the temperatures just above O° C_some of. the bond's are_broxen producing ae Ths jsJe See aca eee eee ee [the demperature of anbedy—of open Loch -of-werter suchas a pond, Jake loc river 18 affected by the temperature eae ait above +the water, reached where the water nearthe Surface freezes . “The ite so formed than, oats onthe surf ushere it the _yecter urther heat loss. Consequentti id water in hi i ae life can survive. es eae & hous fish, bacteria and other nisms Li . actuall inthe water nahi remains Tala ee “Cohesion and Adhesion of Water Malecutes The attration between molecules of -similar substances. is called. Gohesien. ding gives uator ceneiderable cohesive properties thus water [molecules stick. tog ae ppt ae attracted tp other polar molecules . ‘The attraction between molecules of digeorent substances is called Adhesion. Thus, water moteoiles also stick 4¢ other surfaces such ag the sides of Its feiss seein Getta SUS es Tale aes ese “the cohesion of liquid water iS sponsible gor te surface tension. Water {molecufes have a much, strenger attraction 4o other water wolecules than lo molecules in the air. An air~ intecgace (uaterface) [ab an oir-water inertace , 0.4 co dhe surge fa pond, a unter melecule on _below it but not with air molecules bove-it = he unequal distribution of hydregen bonds preduces a force called’ Surface He All of 4he budtegen bonds in wafer at the surface and deuonward resulting the the water to cling or stick dogetier forming a. ir Fill of elastic skin that is diggicult te loreak . “The result is Sone. aquatic organisms can walk in wafer ane oan remain, suspended. Ke undersice of dhe stin. e cohesion of Liquid wmter, as a result , is responsible for tks urface fension.. Water. has a qreater surface. tension than other Liq ¢ adhesien of liquid voter fe cther gubslanceg such as glass. responsi b tor capillary action. Ip a alse tubo with a narrow! diamete placed fa beaker of umter, dhe unter ull rise in tfe qube above plow of witia in the beater beause the adhesion of valor bth gos curface.drasing fie force of grav sohioh d devon. it_upward_is st he _nacrower ecfrostatic ater_and the alas: igher Re wafer rises . [Caplllarity s¢ waiter is one a biol alleas high trees “fo -ranse ‘water from stheir_rovts to their leaves charge distibution within a mo 2 Tn water —_eerre lightly negative 1on the other.Carbon has feur electrons 1 Organic Molecules = = [Organic metecsles or organic. compound s Compounds that contain the olement carken are classified as Oraanic , and all-cthers a8 ‘inorganic. The: human body containg lar. Calls contain erganic molecules. 4 vag eutermost shell and -this allows ik to hond with as many a& feurether atoms. Merever, because these leonds are leovalent, they afe quite strong. Usually, carben lends 4 nitrogen oxygen hydrogen or ancther carbon atom. “The ability op carben +o bond with cther carbon atoms maxes carben chains ef varieus lengths and shapes possible - Long chains containing feng-el_50 or more carton atoms are usually fund “in livin Z 0 42 carbon bending goemetimes results in ring ‘compounds of bilegical significance. | USE | oto Caaf hase! King. cxmpound (Benzene). a—-—¢ Na be cs m aes 1 # Small_melecules have functional groups = ‘The small organic molecules in living orqanioms such as sugars, amino acids, fatty acids jand cucleotides all have a carlaon backbene but inaddition ei functional groups such as the hydroxyl , carboxyl , phosphate ups. “These functional groups determine the characterists of small equnic _ molecules: One characteristic of Sone scganic mdecule vf some importance. is whether ib is Iydrophiltc_oe hydrophobic. BsAldel hyde qrup R= GaeRe Ketone group: oni she eau R- OH Alcohol _qreup mG Carbtnu\ aqmup ee | ~ OH Kc or i Re 0 r = on Phosphate group OF _ Hydrophilic molecules have O8 .Sultil oth STUCCO Renee Glucose is synthesized ror KETTEIACCNAANNREE. in. plants cn (Os + H.0 see CotaOe +0 [Solid euqar form crystals and discolve in water 40 form a cuect — sting solution. Sugars fall inte jamel: aa hacia Sugars are one

a H= 0-H 2,3 dihydioey propanol . | 1 =vtt = “ ae risce cantaine shree oxrbene. Trioses have «ST TESeTg,| oa Dextrorutatory Levorotatory | & |When a lunits, ib 12 called an As a matter of fact , 0 carbon otom that is \ emu la units alled a Learlbon atom . {Tn monosaccharides attached . The t pm _uthich case He menostctharide js callect an or.is [qoup when i is called o |Types of Isomerisin Figure 2.1 H-'c=0 AN Leverotatery - Qiyceratdehyde er _L— Glyceraldehyde. AGERE ERGERSESAANGRA RCRA tere = cv ROISERISRRNCEISOTNAREANS 7. the Same compound ( NACHYCRENESRNpEURAS) Dextrorotatery — Glyceraldehyde oc_D — Gixeeraldehyde where = ithe* Jn Ketones , the Suaars exhibit various forms of Tsemerism. J As the shape of an organic molecule is crucial, the way the afens are ‘ocranged inthe meleciles is as impertant-as the type and +he qumbe toms _pregont- lec mber of pascible sterecisomers of a compound depends upD and £ Tsomertigm. he designation sf a suqar isomer as a. Der its ae image asthe L foom_is Aetermined_b y tks special relationship to the pa ent compound of the carbohydrate family. The L and D -ferms of this Sugar are shown Lin their respective diagrams on the previous page Figure 2-1. Lon Hee fampousys «When ¢ __|selution ee {(aerberetabory) orb fe leek iia oidHexoses The structure i a i i etructure of Gluense ean be represented in B ways. (Cals) 1. Straight chain Ha'c=0 agen A Ning roaaieate ees 1 Kk H | » ‘ 2 oT ali on Higa elise? ss ar at wae ot i es 5, et " Ht 1 w-c—# \ #Galactose (Aldose) Glacose’s coayersion a dg sion gormohomns Seat © Ti Sbiaight: chain form He ESO 1 Glnevse's cing form is call eal Pyranese - a* [Tn water, chains bend te produce a ring form Fructese in its cing form _MaKes a Furanose Ring. Galactese in its Bag, form makes @ Fuyranese Ring . al4 |e, carbenyl quup and atleact tase hylroxyl groupe (ok). 2:4 fruciase have a earbenyl group en catbon-2 lecule, and ave therefere. ealled Ketoses. __|Hexoses axist in three forms , the. straight chain. , the ring -ferm and a __jehain form. To _fornn he link, a carbonyl group reacts with one of the roups el ain carbon are Stitt numbered [aS they wee in the straight chain form. “The carbone ene (3) is alunys, in drawn on the right handside Fructose Ns of isomers : Q** Ue a 26-2 QsLsomers of Hexoses D and L isomers; these differ from He total number of isemers - __carbeo: | adjacent Olsen caren adjacent: todha terminal grup “one right maces Naine 2 D = Giycoraldehydle si Namé i t= Gliyceraldehude You have to distinguish between tse dhings i 1. Determination of the number of possible isomers of hexoses la Determination whether the hexoces' sugar issD or | isomer. [The more important isomers found usidh alucose are as follows | Dand L isomerism.— Eat | \ Lae zs a Te Ss Pyranese (hexagon) Furanose (pentagon ) | “Two -tupes of fings can be formed ._A ring of six atoms i called o [Puranose ring whereas a ring of give atoms is called a Furanose ring. 3 he purannse ring ig the more stable tinteeormed for aldeses (aluace cine mafe_stable'ring}formed for aldeses (qluone_ and galactose) while the puranose ting 1s more stable for xetoses (gructose) HOH Glucofuranese. (Fe Shacse # = 1 I 40H ———o * f- OK 4 y Tot C 7 2) i 4 # CHAO eat te i on R Frietofurancse Fructo pyranose (ibis not table)3- Alpha and’ Beta (A ond B) CHADH & et X= Glucose B= Glucose (alpha qlucose) (beta ~ glucose) Glucese Forms two isomers . 1p the hydroxide grup en carken—{ is below the cing, this will gorm an algha- glucose hydroxide group on carbon — 4 is above the hic will gocm_a: beta~ glucoce . lq. _Epimers,Pentoses He c=0 1 4 —"c=0H T Nea rt =O 4 Ribose (Cs Hie Oc) c— OH {Fig 11 ‘The siruckure of tui common _pentoses shown above. [Pentases are menoscacharides uit fire carbon ater “hey_have He simypl _igormulas Coin Os , carbony! group and atleast two “hydroxide Pontoees exists in beth chai. and_cing form. [Essar ene MME cirdeiural german. cA Re mpetant and sloose and deoxyribose in beth the straight chain and cing ¢Both devxuribese and cibese are stable in the form of the turancse ring. ia SS Fiqure one also shows the small diggerence in structure between ov ribose molecule and a deoxycibose molecule » [The deoxyribose molecule hasmone less oxygen on carbon -2.. This very small _diggerence has far reaching consequences in the same cell « S_focm RNA and deoxyribose Sugurs form_DNA. RNA anc DNA have very different functions jn the cell: DISSACHARIDES Two _monossacharide molecules can be joined +> makea discacharide | molecule = forming a bend between two monossacharide molecules by {eliminating a molecule of vcter | | | | Ci. 0. HUGH 0, a anor cit, + 10 or. Dehydration reaction “ott chor |This ‘ype of reaction where a bend is formed) by the elimination of & water (0) molecule is called _a Condensation. = Glucose piper ¥ IFA Glycosichie tend, Lactose.Sucrose While a 1-2 4s from he carboa atom 4 ae monegacharide to carbon- 2 of Hw second monosaccharide. > & ~ glucose = fructose ~ [teeing 185" Tand-invertt = ¥ a oF ‘ructse 2-2 Glycocidic bondThe hydrogen. bend stabilizes the helical shaoe of the Amylose -| 4 [Starch is sound in two forms, both ames fom x= glucese resideres- starch isa polymer formed from x - glucose monomers. Starcl. caw. exist in two forms : a. coiled polymer ora helical shape witout branches A if As called Amylose. Tt has another form called Amylopectin. ~In_amylose Ane alpha glucose molecules are joined loy 1-4 dycosidie ___ bonds. “The angle formed between tte C-0-¢ bonds, er between the rings_is Similar to the angle of water molecules about 107°. Mis angle means that the polymer is twisted inte a helive (a like \spiral_ staircase). The iudlteide qcoup on he carben-2 of eacl. qlucase residue grojects into the middle cf tte spiral. This hydroxide qreups [orm hugliogen. bonds whith each offter which ctabilizes-the chape of Ae amylose polymer, holding it in its helical shape 2. Amylopectin Tn_amyno pectin , the alpha —qlucss€ monomers ar _jeined by 1 i qlyosi onds, and 1-6 glycosidic ‘bonds, each aime Wtitekamie Aieatea bond, a branched pein 4s puk inte the polymer. “The branched paint ecaurs every 24 — 30 residues. snaking a_multi-branched , comoact polymer.DRO vee) [| yr ree ERSBoth forms of starch are very compact. Amulose is coiled-up into a compact helical shape and amylopectin 1s branched te forma closely packed brush. Shape » [The function ef-starch is to act as an energy storage_molecule in plant [eels and the compact shape means that manu qlucsse residues can be [stored inassmall volume wiikin the doll as well assay ce Avec ti co les into a polysaccharide reduces the number lof small molecules inthe cell. “This is important: because water entecs the il_by ssmosis and the more eelis molecules ‘inside “He coll, the more concentrated the solution inside the cell and the more water that will enter by osmosis iS sal |Stoxine dhe. glicose_as starch means that the solurtion ingide he cell is lest concentrated and so, less water will enter by esmosis. Storaq' e Folysacchat ide 1, Starch ——_ ae co Starch is formed of an alpha. glycosidic chain_and such, compound yielding. only “alucose ca hydrolysis ts called Qlucan. Tt is the most important food source of Carbohydrates and it is found 4n corals ato s and other vegetables. i “The tun chief constituents of starch are amylose representing 15-20 nk whic! son branching, helical s shructucesand amylopectin fopresenting ie 25%, which consists % branched chains composed of 4-30 glucose residues united by 1-4 linkages ‘im the mam. chains ond _by 1-6 Yinkages ot the branch points .alycrsictic veaite aod 1-6 qlycosiclic bends. j ase al polymer is branched Lie amylopectin but the bench pei focal condition.5 { Cellulose Relymer of a PB — glucose monomer aot ow ( i ea P-glucseae gh ; AC. N = ‘ em | a Leah ON A erdency hoe acl imicrogibril Cellulose is formed from B—glucose monemers. Tk is a pelymer of P=qluesse tonomers_joined_by t= 4 glycosidic bonds. Tn order do make He 1- 4 esidic bonds, eve nd P= glucose residue roust be turned upside _ wn. As every seand residue is upside down every Kink that bends the gslymer one wy. is cancelled out b ext Eneabienancteaa! opposite direction . ths means that a polymer -ferms a. straight chain. As there ore only 1-4 glycosidic bonds, there are no branches in He polymer. These Shaight “urloranched plymers_come “gether ‘te frm. _| Microgibrits - The polymers making up the. miemgibrils are held together boy hydregon, lends bowen adjacent chains» ‘The cellulose microfibrils are very strong wen dhey ate subjected ty a. pulling force along dfeir | and This makes “ther an. excellent lou ding material [Humans have found man nyases for cellutose . Cotton fibres are almost __ pure cellulose ing. Furniture and buildin ntain cellule:Most onimals , however, even humans, are oot able to digest cellulos: are: a re nable to break “he For_humans Pte ae a Source re Stare and fibre. Cows anc Ee ive starch and nuttients fram grass because ‘they have special stomach bere bacterial can digest: cellulaseLIPIDS Lipids are extremely diverse group of molecules , Unlike polysaccharides liistdeeare “not polymers cather they ace quite smatempemtes, hat Jhave_streng dependency to asseciage Aeugh non covalent forces [Lipids aw ‘ucually characterised by a xind of structure shes in Figure 1 betowr. The structure consists of a polar hydrophilic head connected to a. nen= polar hydrophobic hydrocarbon tail. Lipids are thon a og dhe molecules which are called itvel Empirical formula. CnHanO © CoH, COOH, er © Cote 0; (8) | Unsaturated Fatty acid. ° c Empirical formula for an un-saturated. fatty acid with one EM Asuble 4s: Catg Oh, + Cats CooH or | 2 Cate Ji it poe Hind.a KINK , as shown in ©) on the previous page - {In figure (A) on the. previous page he a formula gor Cal ey acid hydrogen atom bonded with carben- 4 at the very ‘ail of the fatty acid. Asa result _,an example of an empirical formula of a fatty acid lis CaHis COOH not Ce Hy COOH Empirical formula for an un=saturated fatty acid with 2 double bonds & Cn Hanna 0 Empirical _formuta foc ar an un= Saturated fatty atid with 3 double bends is Cn Ben-¢ Oz [en tance Os. The REIRIBIESEMINBlels oe the FAPEMUBEIE which are also constituents of See are. ee saturated (c- — Si, to. ace. single bonds .[saturated fatty acidls |The most common unsaturated fate syacid ts Oleic acid sith one double. loond between carleen -4_and_caclasn= 10 + [The number of double bonds in ar id varies goon ene tp four (1-4). But in cl evi fia, this. one with no deulole tty acid (one with ene double bond) is CnHan-20 i “The empirical formula _for an un-saturated. fatty acid (one: wit shoo [double bonds) is Cn Manag Oo. ae ee aan~ satura’ catty acid (one wits-Hiree double loonds) is Cn Henne ] “Toble 1: Formula ef fatty acids Formula sf fatty acid Melting Point (°C) 1._Cie Hag Oo 13875 oe = 2 Cra Hys Og. 36.0 3. CwHss Or = 660 A. Cty 63.1Lf # v~= a ho ! | = V8 Ley-§] ell ) ty BAW hag —Y-O 4 Ww ' 4 a MWWiy | é x Lt 4 al} ‘ql ! 5 a orpeyn—s | S| a ya) ioe s a FiSEs brimesleca ob 6 fycceal The gececal porrula of brighcecides is showso tn pig 2 Ry Nolen ae Laslnnop warren pally Pearly [lie pliner et peli! a *C, tus (skeen Zeio fois f beeen - Bef lege -ursatucale ane ipl ln en oe Lace bi bce herons ee eer are lhe Ble ere $s STs cabal palke is quilewpicm sald ecpeeial, 3» Hp dedmewchon shai, ; teotp Tie sande chne_porcr He meblag rial dab in lable 4H easea_ lacy scbvraled chon eae osha feel be fo steel inerystaltes sbevelvees, -by conkrast bad op =pis lacbbe (haploid) (clerphlpd) Denepolec bail group R 3 [slat RIa ads debate dale, BS ble Nee S AL: Fev linea tat ey rl HetWin Wares are esters of long chain alechols uitta long chain atty acids . The | econ be viewed as having a weak poor food group and Leng non-polar tail Fatty acids found in waxes ore usually asniftabels wheres uloofuls fund An waxes: may be saturated or unsaturated . 1 [Waxes are ighly insoluble due to the wenk polar natufe of Aso result is class og molecules congers water repellant characteristi to gnimal skin, leaves of cortain plants and to birds’ feathers. “The glossPROTEINS . eee age very complex ules kg eee ee a fs bi and. . But lin addition, proteins _cantain ae 16% ican Sugar j present in many prcteins, and other minerals ‘ait as Iron (fe) copper Toding (1) and froschorus (F) are present in smaller amounts. Proteins make up a. high percentage of the structure of living erganlem example , about elena also tave part in the fundamental Es with its on_unique +hee=dimensional_structure wich enables tt to carey cut a specific function . ‘Simple organism: quck as bacteria have about 1000 diferent winds g lorteins molealas in Keir cells. Humans gobably have between Se6cD . ‘and 100 060 _prtein molecules. oie oe ay mani eeontl ee Enzymes Bicloqical catalysts Hydrolytic enzymes, Biclogical catalyst: ‘such as Amylase land felymerase «| Defense Antibodies 1g (immuno — “To recagnize seein let = Gamma) microbes and oa | Kan antileedy) lets. Transport Globular Protein |osmoslakia Cortes onygn(0) ] i Myoglobin fl (a) 1m muscles. “ee itd tin tend jbFUNCTION CLASS OF PROTEIN] EXAMPLE USE Structural froteins Fibers Collagen [Wioves up tendons ancl Ligaments. Keratin Major cempenents of hairrand cellspails | Fibcin. Blood clot_- Muscle | Actin and Inyelvement ‘va | Myosin [movements . They enable muscles to move. Signal Proteins. Ensutier Hormones} Insulin Anvelved in cxtalling i —alucese levels inthe blood . Regulation as osmotic | Maintains esmetic. regulation Albumin. Serum albumin | concentration of. 2 Si loleed . —_—__ Proteins are used as fuel especially during Stafation and fasting but their main function is as a source see amine acids. The amino acids are used othesize new fowth and repair. 20 amino aciels are needed Ly humans ‘i of which can be synthesized by ae body and are termed as Non-essential Amine acids. “The remaining [4 amino acids must be obtained fiom-the diet and at aillad Essential Amino acids. One of these essential amino acids is called. Histidin which 1s essential for ingants , small childien and adults. he bed cant. store excess amino aids ,so we medaka regular ed of erteing in our dick. However, the ameunt varies wich oge. {Animal prods wets, meat of. proteins because thes, contain all He escential amino acicl¢. These are fealled_Comglete amine acids, ‘ There is, and only sheuld be 120mg ef glucise. per Imm? 6, bloMoSt plant roteins are incomplete kecouse they lack ene of moe essential amino acids . Nevertfeless , all the amino acids can be cbtained af a ° |Bating & mixture of beans and corn for example can obtain all te 4 essen amino acids. AMINO ACIDS = General formuta of an amino acid, ‘ Be a z e oe be et en i a aa a R Sageo ai: Noy COOH = Carhoxyl group (acidic) K NHg = Amine qwup (basic) R sicle chain grup ‘Tryptophan.+ we : a n o . jaMine al a Alafiu ae = Nok (non-polar amine acid ) i : po cece OF NN it ering ua (causal _(folac-amiao.acid ) 4 A molecule that hasa positive end and a negative end ‘called a Zwitkerion . contain. twp reactive qrmups and amine geup and a. ae grmup. ‘There ave 20° common amine ociels foun an organisms and these clipper prem one another esition of he older chad. to carbon 2 which is alled “the R= ns he ss group varies iw ates prom atom found. c und an, CH, dan kine asst setae Ainyetophan: Most bakteria sor L ~stercoisomors of amino acids, while| d= alanine L = alanine Carton - 2 ‘s jpined te four digferent_qoups in amine aclds except Lycing - Thic means that all_ amino acids except qlycine can make ster vis soMerS- AL common amine acids in_mammaliqn sqjanisms are L -amine acids ‘rather than D= amine acids, but D-amine acids ow found nthe Pais hi means Hitt amino ede 1a He properties of an d and oropertis Such substances ate called A i Ab the PH op Ge cell about neutral , bob. the aming group and the |carhexyl grup are Awnized « = coo > coo + 18 pod! charged at the offer ¢ pe ion an aeA Zwitterion is a molecule witha positive, group and anegative : gnup ib is a double ion. = Nie eee | 1 7; ; fa fi = R= ts ton= polar wil 2 COOH ae A\ nouteal solution Anionic form |) PH= Nie see iit ciemeilliatbanat 2 An z ‘Reidic solution Ee = | ON-wis iu tons in \ COOT In excess COO COOK (PA>4) Dipolar us (Amphion) 3 Roles of Amino and Carboxylic groups ef Amino Acids . [While the R~ groups of different amine acids vary, the amino and aarkoxylto | gfoups ave commen “p all. These. qeups aie important dor tuo reasons } e Shay As shown in Figure: 1 above, they tend t> disacseclate when dissolved inte water < that many amino acid meecules become dipslar ions, each eentaining negatively chargeal corboeyl (C007) and positively charged amino [NH,*) groups. These tons give.a sclution of amino acids a “uggering” eppect re a solution which balances changes in pH and ‘tends remain at, or close 4p, nuetral_pHt. Tn neutral aqueous solutions, amino acids with non-polar R- qPups exist _as digslar ions called Amphions in which the carboxyl donates a hydragen wn shaugh che amino group - vAmino acids can therefore_ackas donors. and acceptors of hydregen-tons ond are here sald to be Amoheteric. An Amphoterie substance is a substance that has beth acidic and basic 1 orepertios . a Amino acids change when the elt is varied. In acidic solution ashere the +7 ten concentration is high, the negelive corkony| (00) group it able 4 bind Some of the hydrogen tons. forming gations while in an alkaline solution amino acids donal hdragen ion f from the gxsitive amino (NZ) grup to he exress hydroxyl (0H) ions forming water molecules andl 4 ons: The ability ¢ Substances: such as amine aciels 4p control fructuations in | ptt is cated Buftering Opacity. ; | The equilibrium geint for the reaction legends en the bye 80 | cencenttation | -———__—__—_____—— | | k=amine aed d= amine acid, (peptide) Ca pepticte) 4 | [free amino rer peptide i digebtides (sth one peptide bone)| Short chains have 9 amino acids ¢.q Hormones Leng chains can have ten thousands ( 10,000), of amino acids. | eS : hi* 3 ages H, L o F N—c—c + T 4 on # Ls d=-amino acid Aitpeptide ets La Re LH. yey 5 |} oo: [| GN=3C— ¢ = NO Cee + H.0_ LW 1 LA leet oH | x pert Ca oooh aut peptide = veil : per Hence : Tripeptides + amino acid ——> Polypeptide Tico amine geld molecules con ‘pin agether in a condensation reaction in ich a molecule of water js climinated. A dipeptide is sormedl and “the bord between the tuo amino acid residues ts called the peptide bond Additional amino-acids can react vith a dipeptide to ferm fitst a tripeptide and then a polypeptide. NOTE > When on_amino group (Nip) is joined tp carbon 2, the amine acid is called o - amino acid (alpha amino acie )ISOMERISM LYSINE The chemical structure of Lysine anc its igomerism. - Cu,+ CH, + CAy+ CR, — NR, ) &-g3eup Ws | S side chain | ee a w i ou 4 OH Ses oO oO oH oO Z Z t 1c iS sec | I T ica 1 aa ! #— ¢ — Np e—E—A Ch eS . oh '—¢ — T wry ¥—f—-F ie cu quietly I § Ny NA, a X= amino aciel B-amino acid Y=amino acid (Alpha amino acid) (Beta amino acid) Gamma. amine acid ) 4 osamino acid (Delta amine acid) NR, E~ amine acid (Epsiton amino acid ) Carbon ~ 2 Carbon - 3 Carbon — 4 | Carben - S Carbon — 6 | PosiTIoN oF NK, RARE AMINO ACIDS. Net all amino acids are alpha amino acids. Any molecule cornining beth and an amine. group is_an Amino acid. Alpha amino a carboxylic grou acids have the amine group en carben-2 but other amino acids have urther away from the carken- 2. he amine groupon carber- 6. These amino acids clo not join together to make proteins , but some of the have important functions in_organisms . For example, @ ~alanine és the building bleck for Vitamin 85 which is one of the chemicals used by cl as neurotransmitters . TClassigication of R- gro mine acials R=grup: at | | charged! un-charged (neutral) sl 7 ves Polar Nen=pelar ‘Example ¢ Example > Sane erie __ Atanine auch as Guta sich as Lysine r su acid 7 Ok si MV p en nc ChyecH¢ ee Vee oH Teal gu ee 7 = eZ SN=e—c i Hee ne OR v Ciro | c T | # Tne difgereat R= groups give each amino acid slightly different gogectyes. Fase R~ quups a very imporfant: lequse ey a1 unageected wfan “Re anita acids, join 4» make-o. pulytooptide and contribute trward dee paperties o¢ He ply eoplide. ta. digeerent R~ gnups can be dassigied according tp whole ey are dforged or uncharged (hexhal), uncharged paar ot cencpolar, a8 Re PH of He call = [Some of He R~ groups wall havea gositive. or. negative charge a: as fhe Pit ete coll. “These ax called domed groupsAn example 2f-an mine acid wit a eolar R= Group is Serine , which has 1) up within les m1 An example of an amine att wie a non-polar qmup is Manine, die IR-qoup of wfih io a “dingle methyl qeup. —~ 1 el aero pa Polypeptides C-terminal, Pend depending on the amino acid residues present A chain ee amine acid coe Hin. gether to fea a _plymer, ig is e ly|The pelypeptide has a backbone dhat cuns-the lengt@ of the macto~ _ [molecule As the only digeerences between the algha_amino e-acid are the R=gnups. his loacxboone. ‘The polypeptide baccbone is flexilble and ean corm Indo a variety of oda-deiacbh Joes shape. hydrogen, bends can form dicteran saris oC lee eolypeptide loackbone. Everytime the hydrogen bond _forins. the polypeptide beames a little ere stable and the mest stable shapes are those which contain the must hylrogen bond... A__protein's function depends on its spegizic conformation + mate pelypepticle back-bene "ss Wan der Waals ferces i) Fig 1.2 Cross-linking within a polypeptide| Examples of hudrogen bends in Proteins | “Type vf hydrogen bend «| Hydroxyl —hydroxyt Hydroxyl: - carbonyl Amicle — earbony) ~| Amide — hydroxyl Amide - Imidazele NitrogenWe spieieinicoie Deidetelledlcab axchetnuer aminabactds, ined _by peptide _ lends ina Specific sequence, However, a functional protein snot just | compact shapes that cemlain ceils , zigzags , turns and loops. iA numnloer of factors constrain rotation areund thecevalent bends in a polypeptide chain in its native conformation. “These include the amaght presence ef wank chemical forces which are + G) Hydrogen. bends (3) Van der Waal's forces _ Ga) Tonic bends - (au) Aydeophobie interactions , and _ (¥) Cortain covalent bonds guch as the disulphide lan les sormed leetween, 4we Cystine amine acids. ~ ‘no acids tina ill determine the Ahree ‘The sequence of amt sn y the = tae. Many. protel onal on.Levels oF protein structure There are cour levels of protein structure 5 namety Gy Primary structure = (W) Seeondacy stricture. Ga) Tertiary structure (Ww) Quatenary Structure [paimarRY STRUCTURE OF PROTEINS Lysine Valine Phenylalanine Glycine Arginine, Cystine = Glutamate Leusine Alanine Methaonine Histogene Fig. 1: The: primary ctructure of Lysozyme ‘The primary chructure of a protein is dogined ag a sequence. of amino aci that mate up its gelypeptide chain. This —_ B SS pics st te cite ing Siiauiiae wactanes pradicts At equilibrium , the rate at which A and Bare converted to C is equal to sthearate at which Cis converted back t A and B, The [position of the. equilllocium depends. on the energy difference between the __|reactants and the products. Enzymes do not change the direction of ihe ceaction’; they ,hewever, speed up the cate af which equilibrium is ceached « ‘ |All enzymes are proteins and such have the properties of pruféins s () they are. polymers of amino acid residues . i) they ace denatured lay thigh temperatures and extremes in pt. (il) they have three dimensional structures that awe uniqu £ gocticular putein. (w)-their_ginal shape. is determined by the sequence of the amino acid ~residues. (V)_some enzymes. require non-protein groups to function effectively.[Enzymes are different rom ether catalysts . Most inorganic. catalysts catalyse a. series of actions. that are inuplved. ___|with similar substances _ Enzymes, however, are very-specipic 4 they, cataluse only one gacticular weaction » ‘An enayme can distinguish one hexose ™Smgeraein- anether, one amino acid ‘srom another, one nucleotide trom another — this specificity is very essential as many of the metecules within a cell ace chemically very leimilar, digrering fm each offier only by the pesition of ene small gin log atoms, Each enzyme has ai gpecipte substrate nthe substrate is the gubstance that interacts with thé enzyme and then reacts. prducts and. give to interact again wH& more substrates. pee to At gan at the end of the reactio _Delailed shidy hos revealed that mast enzymes have at substrates they interact uth jant that ent cules tan mall ortion of the, mes inf direct contact withthe _ is reqinn 1S binding of the substrate eccurs - Th ris bute op the site TE an enryme. loxactly the right ene shape to [git ate substrate I Fig. At Le [see eed Substrate arrives atthe active 1 Substrate its inty-the! Products leave the The env entyme has hole that's (seartangginent op the | Fischers Locwand Key Wypotteesis "active site where tha) active site. ‘woaleeules teeurs.te r ‘orn oducts. This | Nis called Enryme—_| {Substvate Complen ' wal \ukich salostrateinds} ithe active site.There are Awe main models of enz on i Key hypothesis and (ti) the Induced Fit hypothesis . __ | receive further subshate molecules. The Lock and Key hypothesis is a very powerful model moclern hypethesis ‘that has helped generation stientists to hin k clearly about eneyme - i ions Th ei with Emil Fischer who in 1 that the enyme was bo tht would aly be opened bya leertain Key ,the specific He further suggested chat there iso sa 2 Tiglce enzyme that is specific witha sixed shape, ‘The Keyhole is called the active site. “the active site is where the substrate binds to that enzyme and where 4he reachion occurs. Theachive site: is exactly dhe tight. shape to bind the substrate molecule. “The substrate binds 4o the enzyme like a key fitting into a lox. Onée-the substrate has bound do the active: site he waction -eccursanol products are released tewing the active _ site free. Fig. 2: Diagram +> show Keshland’s induced fit hypothesis.besalibacteell as coo” COO" | He Cis ' s = 21 cw see eS coo" Malonate Succinate Jn 1954., Koshland suggested a medigicotion +e the Leck and Key Tnypothest®, He Suggested that enzymes arid their octive: sites are basicall imore flexible structures than rigid or fix ictures. which were describ Joy the Lock and Key hypothesis. Koshland proposed dala dynamic interaction ecauring- between enzymes and lade egacaiiithen a _gubshate combines wthan-enayme, it induces dagpindinssuyns struckute <0. that the active site's: shape changes and the: change 1s $0 ‘essential. ‘The reach’on ufilelonsttaice-place- wtheut: iL. The amino acid which emnstitutes the active stte are rmulded (chenged ini la. precise formation which enables the enayme to-pergerm tts catalytic role ‘or gunchien_ most eppectively. Keshland called his alternative medern mod ___the Tnducod- Fit Hypothesis. =. The cruetal difference between the Leck and Key hypethesis and due Cee huypetiesis is that (nthe former the achive: site has sigid. structure [shag thal exactly gits-+the substrate while inthe labter the active cite E [changes shape os the substrate kinds. [Koshland suggested that the lock and Key hypothesis diel net explain lerrymes do not catalyse reactions when a substrate 15 replaced by a smalle |out chemicaltsy similar molecule. Tp the active site was precisely Re ____erreck shape b catatyse-He reaction as the Lock and_Key.hypethesis “sugge’ yk Fhe small, should lip or 2 ea “kun her tye ena by the substra les =n Koshland s eee sia Eee ae ad soto ea athe correct substrate. He gurther suggested that the R~ groups necessary _ _for the reaction were not in the right positions for-the reaction. ts occurs when the enyme has no substrate bound . When 4he small melgcules enter+he active site, they do nat fit eae gone St ae shen fhe, conc ubstra ke 2 acl it to bring the provided Bile jat the chan. binds Scientists have compared ci a pared the shape of the enayme carbexy/ peptidase te molecule and results have shown. that the ena me. (astecopi iba cone. “We xc URCREGta ard the idea shat at thang inche threesdimensional (2b) structure eats ; {haa the Lock ae Key Types — fit gree ontoEnzyme Cofactors _ uall_not_wxrk‘As chon in figque 1, cf cofactor usually acts as a bridge bokween the emyme and Us subshate. Often it centibukes A con= protein sis onc enryme + function is called 9 Co-factoc. mS ein ules. Some. aoa are. =e emyme maleate af afl times: of is ‘a cofactor-for the _ enyme carboxybeptidase and de ine ion is part of the .Struchure_of Hfe_omyme_maleaute,hald ta. place by the R-geups reAfe ommsncidvvecldues, an 22a ccmpemmeg ia une _acid res B Another ene, feam, is a cefactoe fora aumber of different mes. includ in chrome oxidase, and enayme in respiration. (These inergante tens Int to mould either enzyme er the eine such complex lean be farmed, hence increasingthe chances_of 4Re_ reaction occuring between demand tferefore “Lacreasing dhe rate of rexction catalysed boy dak particular en2ymeout of of alyse cfibn . e i ide Adenine Dinucleotide (NAD) bring Pe ln enlelalaal Diphesphoglycembe ived Nicotinic Add (Vitatnin B,)). = Enayme | Speci gicity ie enzyme - subsivate empl fo ehh saahrase halag 4, tamplenwntary Shope Ep ATi ve conker oF enayereBecause eatyine and substrate molecules ate 3- dimensional chuchires,, He formation sf an. enryme—qubshate. comple requis Rat He apes. of Hu wactants and the active conters of the encumes are lemente is me and fe canoe! unite (Fig. 1. menon whereby most en2t work. only one substrate js calted Enzyme Specipfeity . _— se One of dhe systems used te name enzymes is based on Re substrate. widh which +e enayme combines. for example, bipases reacts: with lipids Factors affecting enzyme ation __ Enzyme concentration Substrate concentration 3. “Ternperacture - PH ( Potential: Hycleagen ) Co- gactors Tnhibi tors be > a 2 ae temperature. on Enzyme -action er Se : s increase in temp. ~ Weis of catalytic Bf_reauion ase P tit ae. Eoaicn Ceitelicken S ine ee ac 2Ls L Temperature Coegpicient = _ fate of reaction at + °C + 10°c | (810) tote. of reoction at ¢ °C is used to loetween 14°C ond _the optimum temp (8%°C) i equalito 2 or double activity. 10° c rise in tempertture. icon" is used) tp on the hat G10 equals twp £95 express Hte~ofto of.a chemical reaction between 4°C and he optimunn temperature (27°C) ge. 3 he. cate wean enayme rearfith. 1s” dou lielicthe: gree) TSE SPAAB'C meat land chances of their callision into each other is a grater osbabilit reaction being re is increased abeve ‘fas le teat increases molecular motion , thus the reactants move mere quickli Asa result, “The temppradie that promotes makinum actuity Gs referred +o as dhe len scours, despite dhe increasing fo 34c . Bacteria tint lve bs in hot springs csntatn exeyme ost optimum temperatures of 90°C er higher. Smurn fempeatures of about 35°CThe effect of pH on the rate of enzyme catalysed — reactions . = — = ef oN Rate 3 action 1 aor, oa igs Lite Sod te 53 H 2» Ce ae Ss a Steuart lath Fig. 2 1. The effect of pit on the mates of enzyme reactions. sively, “es oe ee eragne~subsemploe substrate 1The_ sir} H_ refers te the concentration of hydinaen t0ns in solutiy ‘the concentration _of. aes tens CH* | agpects the stabi lity et oa econ tent bonds and ca son change tte aes sg he R-armupd eFias in the enayine polygep’ of He_amino acids i che. precise, glsbular_s Se suai ie is maintained a= eae cman Ht. = ups a. chang Re went bonds bear Once the S-dimensional shape. ofan enzyme. malar is altered, tien le so cHtalyst i inepfective ‘ancl He cafe of reaction decreases. nk A, chang Sete Crab idole concentration while a change lw ptt of Q ore plt acgle Mpes a. luindredegold inowease in ijdngen em cncndoio, —Thas chasges in glt can have a geal ‘effection_enzy i __|_ Brack pom dte effect a tering enaymes , cha ation dn change the ionisation o¢ the amin ie es sp em. getes, phi 4“[Tenisation of reaciants can alse be appected. “The feamation of enzyme - subcomple x times depends onthe [function ‘Bok enoyme has an opti rH ais lactive . The optimum most ___ oe 6 de & but there aw exceptions .¢. sin, a digestive Feta DEE a a tron eae RE res enaymes but te active conformation of pepsin ares oe 4e the acidic environment of the stomach. Tn contact, Ldn igestive enzyme, uorking in tHe alaline enurenment of hes usorxs well at pit. Erect of enue Concentration. Enayme concentetion _lfigs\ + Relationship bebueen enzyme ancentration and ae te of. : iayplveatllonne Sota: 9 SEPfeovided that athe s tration 18 maintained at an high level ‘and other conditions. such as pH ,tempemture are. kept constant, the rate of the reaction is proportional to she enayme concendeation.. When the \ active centers eubstrate [substrate ] The effect of substrate eoncentration on the mte of an enzyme — catalused reaction: Fig. * Fig. 2 chowS he effect of substrate iwaction when the amount of the enayme is limited. AE lew aatteatalio, q substrate ,there is a linear relationship between the reaction mite and the ictrate toncenhation. In these condittons, the tio of enayme + substre: is high. Consequently, some active contres of eneymes are aluey bind ith the enayme, However, a point is feached molecules (fee for Hie cactantschange in the reaction cafe. ‘This is bemuce at high substrate encenbalin lthe active sites 1 molecules of any gfien moment a rated with substrates Ss. shad it until athe enayme— substate complex has dissociated into products . -| Efpect sf Enzgme Inhibiters? “FE = ‘Inhibitors Reversible _ Trreversible Tahibitors Tahibiters a ~| Competitive Non-Cemperitive - Reversible —_ Revesible pee cil Sclentists studying eneyme —catalysed reactions discovered -that certain substrates slove: fate of waction when they were adde the reaction mixture, These substances called Eneyme Inhibitors fall into «ies ilble_and_@ Trreversible (nlon-reversible) . sReversible ‘Inhibitors “[Reversibte® inhibithrs are cubbtances: ishi joing _|widh substrates. Ackivity of the enzyavensis atv cden ea hibi tor is removed Non ~neversible inhibitors are substances that the activi: dhe enn e cause irreversible inhibition. here are tus types of teversible inhibitors + () Gompotitive and (ii)Non -compot ‘inhibi tors. a ar J 5:pibiter competitive $6! ae Fnac 08 | Ne reaction possible e Pee [Because the enayme a blocked Cengetitive inhibitors are structurely.cimilar( ele te tal fa substrate but they cannot react. The similarity in gructure-and shape means ___Hhat-fhe competitive inhibiter can bind + the anita lout Ut cannot react ty produce ony product. “The active site is therefore, eccupied by the competitive Inhibitor for seme of the time and during this time no substrate malecule lean bind. “this decreases the filimber of reactions eccuting inthe active sites _ Jand slow the. cuerlt rate of reaction. “The classical example of competitive ‘inhibitors {s 4he inhibition eg succinic. hydregenase by matenic adel as ter Fig. 3 (A) and (8) signin Substrate of the enzyme ecinic i ciccrancialte Furamic acid by removing tw H afoms. The eroyme normally releases these products and can then be reused « pe acid eAitive fahibitur CAKE enagme_ by femgoraril The diggecente is that matonic acid ils boron down s-Tin thie particular feaction , the ests nhibitec complex ts mere Stable than the aaa Seat see “This meang that the tio _ or [inhibits molecules ant i a for longer ‘have no_permanent efpecte on the enzyme molecule and the inhibition They_cause can be overcome either by increasing the concentration of. isubstmates or by reducing the concentration o| inhibitor subctance « fy reducing tion ef the inhiNoncompetitive Inhibitors sete an inhibitor“Nenmeam etitive Tabibition ecoure tihen inhibifoc_bind the eneyme lod. prevents the reaction A non-competitive inhi mi 4p asite one enzyme other than die active site. and ib.ietheugh’ that the fahibtar eauées a change. in ihe chape of the enayme.. preventing it fom binding “he substrate, co it cannot react: The. most impertanttype. of. inhibition.n. cells.is.a form of non-competitive — inhibition . Allosteric enzymes have two sites — they have the active ; | inde aubcats. and cnte er molecul inhibit the ag_it & bindin funnest ahi fn at eni inhibit ample of an Allosteric enzyme is pravided by +h |enayme Phesphofructo kinase. which catalysts -the phasphorytadion ef |pruchse G- phosphate tr fructose Fic destosphate This. reack’on ees das Sis_section of he respiratory pathway. When ATE is at high concentration, it inhibits the enzyme shespho ~ __fructo Kinase. allosterically. However, when cell metabolism increases fond more ATP is used up the overall concentration of ATP decreases land the patfiueay once again comes inte operation.Nec small concentrations of chemicals ts! sich os the heavy mefal tons Taxa Siluee (Agi). ond ttercury (Hg!*) and Arsenic (As) or insectides such __- las organophosphorus ; compounds e: farathim completely inhibits some enagmes 1 thaycurine permanently. vith the earyme acetyl cholinesie When ‘it is inhibited acetyl.chaline accuttulate’ and nerve impulses are. _Hoonstant causing, palonged. muse: centration and. paralysis or ts result. eePoE cs Acide Nygro sos ca es | Deoxyribonucleic acid _- Rikenuclete acid i DNA ANA, | There ave tuo typec o¢ nuclete acids iy Ribonucleic acid (eNA) andi, | Deoxyribonitceie arid (DNAY: Bele DNA are! RMA are major be all cells, tagether maxing up fom 5-15 Yo_of their Ary weight - Amost all ie DNA. of digferentiated cells is_present in the oucleu: ag chromatin which gills the entire qucleus of resting cells and (s hight condensed inte chromosomes as soon as +the process of. DNA teplication ts completed. is A small amount of BNA is present in mitechendria and chloroplast which is generally free of pnteins. Scientists agree that DNA «6 a : a Igenetic material and that pure DNA is in dhe form of a double helix. DNA in “the cell 4s oof pure but is conju with a. land coiled inte structures called chomesomes. RNA | | t et Messenger RNA ___RilBephal BNA Trandger RNA. ql (roan) (rRNAY (RNA) ANA ich is present in cee digerent types: ovesenger KAA (mRNA) [Ribosomal _RNA(TRNA) and Transfer RNA (tRNA).RNA is pfésenk in both Ae nucleus and Ae eyoplatn fete cell depdi ‘on es function. Nacleic acids 01 ted to simple prefeins in the form of nucleoproteins ‘The simple pretein_is ucually a basic protein auch as Histone ot Prstamine MITOCHONDRIA AND CHLOROPLASTS CONTAIN THEIR OWN DNA. Celts eae : t “Euxaryotic Proxaryptic calle alte (Tose'calls)) (Not true: cells) [Bacterial as a DNA. Genetic et discovered that Fitechondiid ‘ feic acicls.. and i ate are_free from histone » ROLE OF DNA Ik is now well established that DNA serves as the carrier of _imatedal_in both proxaryotes and euxaryotes. Te ic now Well recoanised that DNA’ is a macromolecule that controls every aspect of cell function. $ Franseripe i TaNSEPHON py, _ Pranstation binsThe_precess of synthesis of protein involves one of the central clegma which postulates: that Hw genetic material info fecular bie lo Te was forwarded by a scientist glows from nucleic acide 4p protein: called Crick in 1952. The gicst stép-apitinic central deqma aes as {Transcription . “The involves a chan cleotide sequences 4>_amiao. ac ils. a and it ig aed Transla: a a ac es Les a very Gs se fy. This is is ci rae role _in hereditar the fact repli molec i that < an. CHEMICAL STRUCTURE OF NUCLEIC ACIDS. DNA and RNA are polymeric (they are. polymers) melecul monomeric units of BNA are called Deoxyribonucleotides and those for RNA are called -Ribonuclestides . | Nucleotich _uacisis ames, [ote Purine and Pyrimidine bases Nucleosides waunek- NucleotidesSTRUCTURE OF BASES These are nitrogenous heterocyclic _hases shi ich are clerluatives ef either a Ze The pyrimidine base he parent-compaund . Tod \ — + “There are three derivatives of pyrimidine bases ° 0 If Th as Gauge PN ee | \ Hu 4 4, | Uracil (U) Thymine (T) Cutosine (C) Founcl va RNA Found in DNA Found in betty slecules nly melecites only DNA and RNAha Purine base “the parent comgeund + There are 2 derivatives of purine bases. 2 Adenine (A) ____ Guanine (4) Found both in RNA both in DNA) | land DNA. and RNARIBOSE SUGAR ©. “S$ cH,DR : ce ra cay a Dextorotatory, Ribose re 6 + D= Ribose (RNA) 2, deoxy D=cibose (DNA) 2, deoxy Dextorotatory Ribose PHOSPHORIC ACID © | re #0 — —— ou NUCLEOSIDES Pade qudleosides — Ribonucleosides “T Pyrimidine nucleosides —— Deotyribonuclensides — RIBONUCLEOSIDES (RNA) Adenine -+ Ribose ———>_ Adenosine. Guanine + Ribose —————> Guanosine Cufosine + Ribose ————> Cytidine 7 pegs Uracit + Ribose —————> uridine, poe » a Parine:DEOXY RIBONUCLEOSIDES a] Adenine +2, deonyribose Deoxy adenosine >) = Guanine + 2 deonyribose __Deoxy quanosine J | Cytocine + 2, deonyribose. Deory cytidine 9 primi | Thymine + 2, deoxyribose Deoxy thymidine [When a purine or pyrimidine base condenses with a Pentese(ribese) lor DeoyPentrse (deoxyribose) sugar, they forma Nucleoside. In, Lease of purine nucleosides the sugar 1s attached t the Nitregen-4 Jatom , uhile ‘in pyrimidine nutlesides the sugar is attached tthe _Nitegen- 4 atom» ae Example of Purine Base Nucleesides. = -witee_—__Nil2__ N > N Coe a ei = 8. a Ra 4 or @ Adenosine | (Ribonudleoside) ] | | 4 | : |NUCLEOTIDES Adenesinte— {Riboauclecsice) i L tl 5 5 { ates 2 Fhospbarie acid N n eZ iv Se Wo — P — oH on Adenosine 5’ Monophesphate (AMP) Phosphotic ester of a aucteosicle0 \ WO— Pp — ot oH | i ow Cutidine 5'- Menophesphate (CA Ribenutleotide )___| Nucleotides ore phosphatic esters of _rudeosides . Nuclectides gall into wo lqcoups: Those hat contain a Ribese sugar goup and dfiose that do not jcontain a deceyriboase._ a base component of the cucleotide is Bonected 2 a 1 of “he nd the structure o a cibose molecule | [=e se molecule has en less, __fuery smal difgemee has far te | Ribonueleotides oe ead __detkeyci bonucleotidtes form _D JRNA ond DNA have very different functions in the cell. [Nucleotides contain one of the five Alternative base components. The ve oganic und in nucleotides are Adenine, Guanine, Cytosi ee ge tA aise aad Cte are pines ubich means hat they have a deub) ring._stouclwe, utile Cytosine, Uracil anc Thuynine ar ¢ pyfimilnes | ehiche |ukich means Hot “fey have a single ring sfructure.. The base ic connected fo carbon 1 of fhe sugar.oO: P= onie — 0+ P—-O-CHy 1 WoL ° Oem P='O — CH, I [gee o nO o & taper eda coe Sad hy * Nuclestides are molecules tes ave Ave miponen tS. a sugar, aghosphate. hahaa & Foro. gels vines hee are two main types of nuclectides namely deokyribonuclectides ave 4 ribese sugar, ene of. the, Seeks uanine “abe or ual and a. phosphate grup. = te 4The connection between successive _menomer units in quelete acids 1s bough a. phosphate residue attached te {he hydroxy) on the 5! carben: one unit and the @ hydroxyl of the next ones “This forms a. phosphodiester |iink between hoo sugar residues. Tn Anis wey, [on ic acid chains do [sometimes contain hundreds of millions of unt® built up..The phosphate ise is strong acid _and tists why DNA and RNA ave called Nuclei acids 2 [Every seeldue Ina DNA or RNA molecule carries a negative eharge at __HHte elt of the cell. Aaa diester ting eesidue germs dhe bacxbone. of ___}the nucleic acid molecule. — Towa and RNA are each regarded as a. polymer made from eur kinds of monomers. he bind belscen egg pine cordon of fla sugar and fe base sitrge referred 4 as a Glyssidic Bond. Sinscytosine, vE ie complementary Fig: L_Anti=parallel_nature efthe DNA strands. (DNA ic usually desig stranded , this means ‘that Here are che polynucleotide hydrogen. bonds. Te weak bonds a “a of Hoh nucleotides £ base. while He other pelyquclestide cans 3° to S'. We cay tatthe two shands are curt ® Finally, when he base pairs form they twist the polynucleetide iat a helix, in which there are ten(1) base pairs for every one Aust” i Double ~standed -DNA is a double helix» _Deuble strandecl DNA is 0 very ry stable ¢ suche iehisiebe because re etic. inform DNA macromolecule can be very ee Exch human chiomessme. Coivfaing-efie long double ~stranclecl DNA mecro- wnolecute, A larger human chromosome contains abeut Oem of double | Strande mol . Working out the stuchire of DNA_f ‘onal ology This ux loecnus® DNA is the genetic matertal of almost all eqns, AML info uild a human and to makenhim or her function is sipced inthe DNA __idhe single cell that ums soomed when the. sperm fertilised the egg. Many scientists have ed on He chemical “composition. of DRA identi the ie seme Aaa ether. wrk of Biochemists the nucleotide uns establi as the basic ee of DNA: structive. Later on, scientists used dey |fechnique o, — Kray Aepeaction SV (1940-1950) DNA double helire Phetogragh by Rosalind Franklin and Mouitice Wilkinsee ae Tn the x-ray diggrachon, X=rays are directed at a ecyelal of a.cubstnre to be shidlled . The X-rays are digemoted bythe erystal and the pattern ete 8 = of make gives Yngor emahion about+the posihions of atoms. inthe _ oe Wiliine anal Kagaiotlh Franild ohiainedaca tala of pure DNA and used X=ray dippmetion techniques. Both obtained a great deal of |inpotmation alaut the structure of the intact DNA melecule and_both. scientists showed that DNA was.o helix Another scientist , Erwin Chargage, used a paper chromatagraph te alyze the DNA from a large number of digferent erganisms. He found Ahak tho amounto each nucleotiole inthe DNA ums-the same pordhe individual of anyone species, but diprerent when he compared the dlipperent species. He conclucledl that wery species had its ewntupe of DNA that uns unique from all others’. He ebserved that -the number of |ourines (A and @) ia the nucleotide always equalled the number of [pyrimidines (Cand T) in nucleotides. He also obserued that the number log A-nucleotides equalled the number of T- nucleotides, and dhe number of C= nuclestides equalled the numberof 4 —nucleotides. “the patterns Chacgage dliscovered are shocon below iin the simple equations just as he patterned -them himselp + lished his results in 1950. By 1951, a model (structure) ¢f DNA. ums. proposed by Francis Crick. and Tames Watson. “They bitilt an achal model of DNA using metal hapes of nucleo _ “The shapes ofthese metal medels wore based on alll the information frm Biochemis Koray diggraction and from Chargagf's resultsz Playing with +he metal chapes provided heir proposed DNA shucture. Crick land Wateon realised thatan A- and T- side by side had+he same dimencions-as dhe @= and C- side by side. Further examination showed tat Adenine|) unald bind to Thymine (7) with Ahe sormabion of. tu hyolagen _ bonds and Quanine (@) would bon! to Cutosine:(e) with three hydragen bonds. However, this. hydrogen ood pairs would enty form ip ene of He bases in each puic ums upside dowo - es the hydtgen Geel base pairs gave Crick and Watson te resolving the list of the secrets “op sDNA- The crucial indin at DNA hash ptlynucleoticles ond the two polynucleotides in Funan opposite directions. “This meant dhat all the bases in. one of the um shtands were —_lupside down and the base pairs could form between the bases prjecti one stand ond He bases projecting som anether « .Measurement: A. metre (m) = 1000. or 10° milimetre (mm) L milimetre (mm) = 1000 or 10° micrometer ormieron (um) Lamiecon pm) = 1096 _er 10°” nanometer (nm) Lnmometer = 10 Angeton (A)Watson and. Crick’s Steuctural Model of DNA _ ~_Arcarding 4 Waten and Criek, DNA_moleoules contain two polynucleotide idhaing Rok ove swrapped helically around cach offer with Be i ___|phosphate chain ‘eutside( 4 ae like coil backbone ef do eee cond aa ines en dfie inside op the double helio © phesphate. abe gwoups. as ransverse le = Me’ ie dae ke. Ieetnseon t acalng fo Xe lig 2 (use) nanometers (nem). Two: purines in in combination use ine more eg 2 naimameters, and tuo pyrimidines ould not: renel all © Re wry actos, but ip a. purine paired gn each case usith a pyrimidine -__ thee “would be a perfeck - pit ‘and de molecule usoutd be dhe same “eM along itsante length. pie a See Ae ladder) would de Aerefore alunys be gucine — pyrimidine combinations . Since a DNA molecule be dReueards x naclectides long, ere is ar psibility of oat Tin she sequence. of bases and variety is one ofthe requi _—_lopnetic_ materials ._ a Me. ase plynudente shanls oe held dagether fy hydrogen kon fines ari ¢_paics ef purines and and pyrimidines. The Ho bends ____ [between _purin : onan a a adenine can bord = 2) H-bonds guanine a hoe Rory Be He lends and so other alternabive ts posi between them. he speci th nd te bends hat oan be. _lassures that for every c every adenine in one one chain there will be Lake offer. For every quanine in the first chain. , there valle? __ lin he other, thw er erect ack | 2 thot ‘evthe sequence of tuclentides in ene chain dicintes dhe sequer lee nuclecticles indie otfiac. The uo stands cun anti-parallel 4o each ther , that is to.say they have /run in opposite directions. One shacy has phospho - diester linkage in_3’— 5’ direction uhile other Strands have phospho di-ester linkage in just the reverse of 5'— 3’ directiondoulte— hele 4 cight= handed and fe lobe Hturn.cccurés every. 34. Angstrom o A= ae ee aalled mayor lqmove , and a shallows narrows one called minor amo. Bott of f_DNA has the following Sequence t s ~TTCAGTACATTGCCA - 3 What is the complementary ¢tand ef this DNA 2 3’— AAGTCATGTAACGGT — S'_TE ven a cimgle bacterial Gall is a complex organism fill Ned with, specialized - | shrackute’ Set te eee envienmontal factors. fin v gor a bacterium requires a cicele. sa circle. ee ri 36 mm that hast pack. ine a. coll that 003 mm. ize of bacteria. |The human liver cells contain 46 DNA nh “DNA molecules whace datal lengl is sup te 2.2 etfes, all_pacved into a. oe ae = 0.00000 1 metws in diameter (the “DNA in a coll must be very well. pit ee poe oe ae a2 sThee is stillia pablem of calecshading how a a of DNA 136mm, in length gitS into a bacterial cell and how Q:3-m_of DNA-fits into Ahe oy eukaryotic icleus oF eukaryotic call he packing must be done in such a way that the DNA docs not break. ‘The circular bacteria. DNA is thought 4» be superaviled, the double helix is twisted and then-the cirole is sealed that the twists do not go out. [The problems vg a Lng mai ad a he DNA aE BGS Eacl. q h i eak ese odd ie the erry ich coll division icrome._ of Ais. ut emeliow a $0000 micfen of DNAs backed dawn 5 that ee 6 4000p times shorter Some gxtcxiing eccurs ute the DNA is axsedabed) with histones fouming, a structuie called Nucleoseme .STRUCTURE OF RNA.Molecules oF RNA are built up fam nucleotides containing the ive - carer sugar “ribose and are always single shanded) Aldteugh lig shand may be eldedbdce on itselp do give an lappareatly. ceuble-standed stucture. All cells contain dfsce important dypes of RNA + The _shuchure - RNA is similar te that of DNA. bout ib digpors lin sas! ay al RNA Contains othe pla ym isk eile mi is a_double —strand ed molecule, oa _ nsideralal exis RNA is also a legs stable than DNA, RNA needs a ‘be less {stable as it acts as a short-term functional mole cule inthe cell ee slapegepesiags eee ee ib ts the stare g etic. Fig 1: Part ofan RNA molecule isa Single strand . Te however, also folds forming small areas that ore double-stranded .essenger RNA. (mana) MESSENGER — RNA (mRNA). a the ‘ingore tion stored in the DNA is-needed for use inthe cell 5 the ingermation mustbe made. Scientists say that He in} is aes tbed_, ond te process is called Transeription. scription uses DNA a6 atemplate for dhe synthesis of an RNA RNA [molecule The template determines the ocler of the cibonuclesticle [residues in the RNA _|§con_the_DNA., is aoe ssenger_ RA [mANA is fe glenn beames asseciated with nlosenes [the _process_of_pmfvin syathes{s = ________ ___|Maleales in the mRNA_are #5 ~ 2000. of nbenucl = es obeniteotides long’ and. long. lnot folded ‘in any special uy. |The “DNA cleotide in @_chromoseme may ce ___louclestide ‘residuesamino acid Ly $ SR acceptor anti - codon acm ‘terminate . A Heterocycle is_a compound that has one or more atoms other than carben in atleast one ef its fings « A Template is 4 physical abject whose shape is used as a quide to make offer objects. [In Biology, a template is a macromolecule which provides a pattern 1 the synthesis of anther molecule