NOTE FOR THE CHAPTER ----BIOMOLECULES---XII

The various types of compounds which are found to be essential for animal for animal life:Carbohydrates: e.g. starch and sugar Lipids: e.g. ghee and butter Proteins: e.g. complex molecules present in meat and pulses Vitamins: e.g. present in food in traces ormones: present in food or synthesi!ed by the body The molecules of the above listed compounds form the basis of the life. "uch molecules of organic compounds which build up life system and re#uired for the growth and the maintenance are called $%&'L(C)L(". CELLULAR ENERGETICS: FREE ENERGY CHANGES IN BIOLOGICAL REACTIONSCellular reactions follow the basic principles of thermodynamics. &nly those reactions should be spontaneous for which *+ negative. ,ll the carbolic reactions proceed with decrease of energy-*+./0but some important cellular reactions proceed even *+ is positive.e.g. Photosynthesis in plants for which *+1/. 'any anabolic reactions proceed with increase of free energy i.e. *+1/. , very common reaction which provides energy in many cellular reactions is the hydrolysis of adenosine triphosphate -,TP0. The biochemical unit of energy is ,TP. The cell obtains energy for the synthesis of ,TP through photosynthesis 2 catabolism of nutrients such as carbohydrates and lipids3 this all occurs through coupled reaction. WHY ATP MOLECULE IS ENERGY RICH MOLECULE? The ,TP molecule is consists of four negatively charged oxygen atoms which are close to each other4 the repulsive forces between them are very high. These forces ma5es them high energy molecules3 actually this energy is stored in oxygen-phosphorous bonds. The oxygen bonds between the two phosphoric acid residues are high energy phosphate bonds. 6uring hydrolysis these bond brea53 this reduces the number of oxygen atoms in the molecules and the repulsive forces between o-atoms decreases3 and as a result large amount of energy is released. The energy released during this process depends upon the products formed and the Ph of the solution. ,'P and ,6P molecules get converted to ,TP molecules during this process. CARBOHYDRATES: The polyhydroxy aldehydes3 polyhydroxy 5etones3 or large polymeric molecules which on hydrolysis produce polyhydroxy aldehydes3 polyhydroxy 5etones3 are called C,7$& 867,T(". STARCH AND THE SUGARS ARE THE MOST COMMON CARBOHYDRATES. The sugar is stored in the body as glycogen -C9
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CALSSIFICATION OF CARBOHYDRATES: Carbohydrates can be classified on the basis of %0 $ehaviour on hydrolysis ii0 taste ON BEHAVIOUR they are classified into 'onosaccharide3 &ligosaccharides3 and Polysaccharides. MONOSACCHRIDES: These are simple carbohydrate molecules which can not be hydrolysed into many simpler molecules. (ach molecule represents a complete carbohydrate molecule unit. They contain < to = carbon atoms therefore their general formula -C >/0 n. (xamples: - glucose3 fructose3 galactose3 and ribose.

OLIGOSACCHRIDES:- The carbohydrates whose molecules on hydrolysis give > to ? molecules of monosaccharides either same or different are called oligosaccharides. They are divided into di3 tri3 tetra and polysaccharides further. (xamples: Disaccha i!"s - C:> >>/::0 such as "ucrose3 maltose3 Lactose3 they produce two molecules of monosaccharides on hydrolysis. T isaccha i!"s: - Carbohydrates which upon hydrolysis produce three molecules of monosaccharides. The gen. formula is -C:@ <>/:90. (xample:- 7affinose which on hydrolysis give one molecule of each glucose3 fructose and galactose. T"# asaccha i!"s: - They give four molecules of monosaccharides on hydrolysis having gen. formula -C >A A>/>:0. (xample: - "tachyrose which upon hydrolysis give each of glucose3 fructose and two molecules of galactose. P$%&saccha i!"s :- Carbohydrates which upon hydrolysis produce large number of monosaccharides having gen. formula -C9 ://;0 n. where n B :// C <///. such as "tarch3 Cellulose3 and glycogens. C,L""%D%C,T%&E &D C,7$& 867,T(" &E T ( $,"%" &D T,"T(:- They are classified as "ugars and non"ugars S'(a s: - which are sweet in taste and dissolve in water are called sugars. ,ll mono and disaccharides are sweet in taste. (xamples: - +lucose3 fructose3 "ucrose3 Lactose are sugars. N$)-S'(a s:- Tasteless polysaccharides which are insoluble in water. They are generally amorphous in nature. (xamples: - Cellulose and "tarch. ADDITIONAL INFORMATION --- MONOSACCHARIDES %n addition to hydroxyl group they either contain aldehydic or 5etonic group. The aldehydic being monovalent is either present at the end of the carbon chain. ence such monosaccharides are called ,L6&"(. &n the other hand 5etonic group being divalent can be present anywhere on the carbon chain. %n natural monosaccharides this group is present normally at the second carbon atom. ence they are also termed as F(T&"(. 6epending upon the no. of c-atoms these molecules are termed as trios3 tetrose3 pentose3 and hexose. Fetose and aldose are added to the prefixes to the no. of catoms. CHARACTERISTICS: - They are sweet and water soluble and when heated they get charred. 6ue to the presence of / -group they can be easily acetylated. They can be reduced to sugar alcohols. They can be oxidi!ed at the aldehydic carbon to aldonic acid. Two molecules of monosaccharides combine with an elimination of water - >/0 molecule to give a disaccharide. They undergo oxidation3 reduction3 acetylation3 react with hydroxylamine3 phenyl hydra!ine and fermentation. ADDITIONAL INFORMATION ------ DISACCHARIDES* %ts main source is sugarcane and beet. These include "ucrose3 'altose3 and Lactose. "ucrose is hydrolysed by both en!ymes maltase and invertase."ucrose is both a G-glucoside and H-fructoside. ence it can be concluded that "ucrose consists of G-glucose and H-fructose. They are held together by G3 H-glycosidic lin5age. INVERT SUGAR: - Cane sugar is dextrorotatory. &n hydrolysis it gives dextrorotatory glucose and laevorotatory fructose. Therefore a e#uimolar mixture of glucose and fructose with opposite signs are called inversion of sugar or invert "ugar.

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POLYSACCHARIDES: - There can be linear or branched chain polysaccharides. Polysaccharides are amorphous3 tasteless and mostly insoluble in water. These include starch3 dextrin3 cellulose3 and glycogens. Their main functions are storage of food. They can further be classified as omopolysaccharides and etropolysaccharides. omopolysaccharides contain same type of monosaccharides. (xample: - glycogen3 starch3 and cellulose are polymers of glucose. etropolysaccharides: - they contain two or more different monosaccharides. (xample: - +ums. STARCH: - %t is odourless3 tasteless3 and insoluble in water. %t is amorphous and white substance. Ihen boiled itJs granules swells and burst to form a colloidal solution called starch paste. %t is a polymer of G-glucose and composed of two components amylase(20%) and amylopectin(80%) . ,mylose is water soluble whereas amylopectin is water insoluble. The structure of glucose is similar as that of amylopectin. ,mylose is linear polymer whereas amylopectin is a branched one. AMINO + ACIDS: - The carboxylic acids containing amino --E >0 group attached to any carbon atoms other than carboxylic carbon are called amino acids. ,n amino acid always contains one -atom3 one 7 group3 one C// group and one E > group and they are attached to single carbon atom. %n a#ueous solution the C// group looses a proton to form carboxalate ion and the E > group gains this proton to form KE < ion. ence in a#ueous solution amino and carboxyl groups are in the ioni!ed form and amino acid molecule exists as a dipolar ion. This dipolar ion is called ,-i##" -i$). ,mino acids in dipolar form are amphoteric in nature. Therefore in acidic solution3 an amino acid exists as a positive ion3 and therefore it migrates to the negative electrode -cathode0 when placed in an electrical field. %n a basic solution3 an amino acid it exists negative ion and therefore it migrates towards the positive electrode when placed in electrical field. The p at which the amino acid molecule does not migrate to either of the electrodes is called the ISO-ELECTRIC POINT. D- L- CONFIGURATIONS OF AMINO ACIDS : - The G- carbon atom in all the amino acids -except glycine0 is asymmetric -chiral0. Therefore amino acids can exist in two stereo isomeric forms3 i.e. 6 and L forms. These two forms are the mirror images of each other but are non-superimposable on each other. Thy are drawn with the reference of glyceraldehydes3 in which the E >-group lies on the left hand side of the c- atom in L- configuration and the E >group lies on the right side of the c- atom in 6- configuration. ,ll natural occurring amino acids are L-isomers. Proteins consist of only L-amino acids. The "ss")#ia% a.i)$ aci!s which must be present in our food are: - %soleucine3 Leucine3 Lysine3 'ethionine3 Phenylalanine Threonine3 Tryptophan3 Valine3 ,rginine and istidine. PEPTIDES: - The compounds formed by the condensation of two or more3 or same or different amino acids are called peptides. 6uring the formation of peptide3 the amino -E >0 - group of one of the G-amino acid and the carboxylic -C// 0 C group of another molecule of the same or the different G-amino acid get condensed with the elimination of the water molecule. 6uring this process a bond of the type C C/E - is formed between the two amino acids. This amide lin5age is called /"/#i!" + %i)0a(". The peptide formed due to the condensation of only two3 three or four molecules of the same or different amino acids is called dipeptide4 tripeptide and tetrapeptide bonds respectively. ,ll the peptides contain a free amino -E >0 - group at one end and a free carboxylic -C// 0 - group at the other end. These are called end-groups or the terminal groups. "ome important biological peptides are &xytocin-nanopeptide3 Vasopressin- nanopeptide3 ,ngiotensin-octapeptide. PROTIENS: - Proteins are complex nitrogenous organic compounds and are essential for the growth and development of the body. Proteins are macromolecules in which large numbers of amino acids are lin5ed with peptide-bonds. &n hydrolysis they give amino-acids3 in other words they are polypeptides of very high molecular mass3 -:/ A C :/9g2mol0. (gg3 meat3 fish3 pulses3 and mil5 are the good source of proteins. Eormally there are >/ amino-acids are present in proteins3 and another six are found in the special tissues. The amino- acids differ in the side chain groups -70. the

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properties of amino-acids depend upon the nature of side chain. The human can synthesi!e :/ out of >/ amino-acids found in proteins. The other :/ must be supplied in the diet. Therefore they are called "ss")#ia% a.i)$-aci!s. Lac5 of proteins can cause a disease called Fwashior5ar. The elements present in most of the proteins are carbon3 hydrogen3 oxygen3 nitrogen and sulphur3 iron3 magnesium3 phosphorous3 etc. CLASSIFICATION OF PROTIENS: - They are classified on the basis of chemical composition. Therefore there are mainly three classes of proteins. A1 Si./%" / $#"i)s B 1 C$)2'(a#"! / $#"i)s C1 D" i3"! / $#"i)s* Si./%" / $#"i)s------ these are made up of only G-amino-acids and they upon hydrolysis give G-amino-acids. (xample ---------- ,lbumin3-in white of egg0 +lutinin3 -in wheat0 Feratin3 -in hairs L nails0 are simple proteins. C$)2'(a#"! / $#"i)s: ------- the proteins which contain organic and inorganic compounds along with amino-acids are called ConMugated proteins. The non-amino-acid group of the protein is called prothestic group. This group controls the biological functions of the proteins. ConMugated proteins are further classified into ----------------------------------------------------Lipoproteins ------these contain lipids and amino-acids. The prothestic group in them is lipids. Eucleoproteins ----- these contain nucleic acids and amino-acids. The prothestic groups in them are nucleic acids. +lycoprotein ------- these contain carbohydrates and an amino-acids.The prothestic group in them is carbohydrates2sugar. Chromoproteins ------ they contain amino-acids and colored pigments. aemoglobin3 'yoglobin3 aemocynin3 Cytochrome3 and 7iboflavin. Phosphoproteins------- they contain amino-acids and phosphate group. D" i3"!-P $#"i)s: - The degradation products obtained from the partial hydrolysis of simple and conMugated proteins are called 6erived proteins. CLASSIFICATION ON THE BASIS OF MOLECULAR STRUCTURE* &n the basis of structure they are classified as Fi4 $'s P $#"i)s a)! G%$4'%a P $#"i)s:Fi4 $'s P $#"i)s:- They are consists of linear3 thread-li5e polypeptide chain which are arranged and twisted to form long strands -fibers0 and they are held together by hydrogen bonds therefore the intermolecular forces of attractions are very strong. They are insoluble in water and #uite stable. (xample: - collagen of tendons3 Feratin in s5in3 hairs and nails3 Dibroin in sil53 'yosin in muscles are Dibrous Proteins. G%$4'%a P $#"i)s:- The proteins in which polypeptides are tightly folded into a compact form are called +lobular Proteins. %n these proteins the hydrocarbon -lipohillic0 ends are pushed inwards while the polar hydrophilic part is oriented outwards therefore these proteins are water soluble and very sensitive towards temperature and p . (xamples: - ,ll the en!ymes3 many hormones such as insulin3 thryoglobins3 antibodies3 aemoglobin3 fibrinogen3 albumin3 and venoms of sna5es3 scorpion3 wasp3 and bees are globular proteins. CLASSIFICATION ON THE BASIS OF FUNCTION: &n the basis of their function these are classified into the following types: : "tructural Proteins > Contractile Proteins < ormones A (n!ymes ; $lood proteins ROLE OF PROTEINS:-

(n!ymes: - ,ll the en!ymes found in the cells are proteins which catalyse large number of biological reactions in the body. ormones: - 'any hormones are proteins in our body. ormones are chemical regulators therefore regulate blood pressure. +lycoprotein and thryoglobins help in the synthesis of hormone thyroxin whereas nucleoproteins carry the genetic information from the parents to off-springs. aemoglobin: - %t contains the protein called globin and is present in the blood3 transfer the oxygen from lungs to tissues. $lood proteins: - thrombin and fibrinogen are involved in blood clotting DENATURATION OF PROTEINS:(nergetically the most stable state of a protein is called as its native state or native form. The native state of a protein is dictated by the amino acid se#uence in the protein. Proteins are very sensitive to heat3 acids3 al5alies and even to the electrolytes. Properties of globular proteins change altogether on heating or on treatment with acids2al5alies or electrolytes. &n heating3 water-soluble globular proteins precipitate out due to formation of water-insoluble fibrous proteins.The coagulated protein is called as denatured protein. The process which leads to change in physical and biological properties of proteins without affecting its chemical composition is called as denaturation of proteins. 6enaturation causes changes only in secondary3 and tertiary structures of proteins. The primary structure of any protein does not change due to denaturation. 6enaturation may be reversible in some cases. 6enaturation is caused by following factors Change in the p %ncrease in temperature Presence of acids3 al5alies3 or salts (xposure to ultraviolet rays or x- rays The most common examples are $oiling of egg Preparation of cheese from mil5. CHARACTERISTICS OF EN,YMES:(DD(CT &D T('P(7,T)7( The activity of en!ymes is highest at near point temperatures. ,bove this temperature the en!ymes get denatured and lose their activity. ,t lower temperature3 the rates of en!yme catalyst reactions are slow because of 5inetic effects. %n general3 the rate of all chemical reactions increase on increasing the temperature. $ut the rate of en!yme-catalyst reaction first increases shows a maximum at about <;- <= oC and then decreases at high temperature. (DD(CT &D p The rate of p on en!yme reaction is complex. The rate of an en!yme-catalyst reaction usually passes through the maximum at an optimum p . ,t higher or lower p than this optimum p 3 the en!ymes tend to get denatured and therefore lose their activity. P7("(EC( &D (L(CT7&L8T(" ,E6 )LT7,V%&L(T 7,8"- (n!ymes lose their activity in the presence of electrolytes or when exposed to ultraviolet radiations. This is because en!ymes get denatures in the presence of electrolytes or when exposed to ultraviolet rays. (EN8'( %E %$%T&7" (n!ymes are very sensitive to catalytic poisons. "ome typical poisons are CE3 >"3 C">. (n!ymes lose their activity in the presence of these substances because these molecules tend to get absorb on the surface of en!yme strongly. (DD(CT &D '(T,L %&E" ,E6 "%'PL( &7+,E%C '&L(C)L("- most en!ymes are associated with some nonprotein compounds re#uired for their activity. These non-protein compounds are called as prosthetic groups. Prosthetic groups may be metal ions or smaller organic molecules called coen!ymes. "ome of the metal ions involved are those

of Nn3 'g3 'n3 De3 Cu3 F and Ea.'any of the coen!ymes are derived from vitamins3 such as thiamine3 niacin3 riboflavin3 etc. NUCLEIC ACIDEucleic acids are another important macromolecules present in the cells of all living organisms.Eucleic acids are long thread li5e macromolecules of high molecular masses. Eucleic acids are responsible for transmission of hereditary characters and for the bio-synthesis of proteins. Therefore they govern the metabolic activities in living organisms. They are present in the form of nucleoproteins. C&E"T%T)(ET" &D E)CL(%C ,C%6" Eucleic acid contains following three contents , pentose sugar - ribose or deoxyribose0 , nitrogen containing heterocyclic base4 a purine or pyridimine base , phosphate group N'c%"$si!"s C The base sugar unit in any nucleic acid chain is called as nucleoside.The nucleosides are named after the names of the base3 attached at the carbon atom number : of the sugar unit. (g. 7ibose ribonucleoside3 deoxyribose deoxyribonucleosides N'c%"$#i!"s C The base- sugar- phosphate is called as a nucleotide. Eucleotides are the phosphate esters of nucleosides. Dor eg. 7ibose- ribonucleotide3 deoxyribose- deoxyribonucleotides TYPES OF NUCLEIC ACIDSD"$5& i4$)'c%"ic aci! 6DNA1- 6E, is the genetic material and is responsible for heredity character of the cell. 6E, is present in the nucleus of the cell. 6E, is the most stable molecule of the biological world. 6E, molecule may be consuderd immortal. C&'P&"%T%&E &D 6E,6E, contains the following four nitrogen bases- P)7%E("- adenine and guanine3 P87%6,'%E("- thymine and cytosine (ach unit of 6E, strand has only four bases. - the number of purine nucleotides is e#ual to the number of pyridimine nucleotides. - the ratio of adenine-,0 to thymine -T0 . and guanine -+0 to cytosine-C0 is one $%&L&+%C,L "%+E%D%C,EC( &D 6E,6E, acts as a carrier of genetic information from parents to their offsprings - 6E, guides the process of protein synthesis in cells - 6E, is involved in the synthesis of 7E,.

RIBONUCLEIC ACID 6RNA1 The 7E, is found to be genetic material in some plants and animal viruses.7E, is found in nucleolus3 cytoplasm and on the membrane in ribosomes. (ach ribonucleotide contains , pentose sugar-ribose Purines- adenine and guanine Pyridimines- cytosine and )racyl ,nd phosphate groups. S# 'c#' " $7 RNA Eucleotide of 7E, consist of pentose sugar ribose. These ribonucleotides are lin5ed to each other by <J-;J phosphodiester bonds. %n this respect 7E, resembles 6E,. The polymeric chain of ribonucleotides forms 7E, polynucleotide strands. 7E, is single stranded except in certain viruses.7E, doesnJt form helix. The primary structure of 7E, differs from 6E, in the following ways: %n 7E,3 the sugar residue is ribose3 whine in 6E, it is >Jdeoxyribose 7E, consists of pyridimine base )racyl-)0 in the place of Thymine -T0 in 6E,.

C%assi7ica#i$) $7 RNA The organisms which have 7E, only as nucleic acid use this 7E, in genetic mechanism. "uch type of 7E, is called as genetic 7E,. The organisms which have 7E, along with some 6E, 3 use their 7E, in carrying out the orders of 6E,."uch type of 7E, is called as non genetic 7E,. The non genetic 7E, is heterogeneous and is classified by cellular location MESSENGER RNA- 'essenger 7E, -m-7E,0 is short-lived molecule that carries genetic information from 6E, to ribosomes where protein synthesis occurs. RIBOSOMAL RNA- 7ibosomal 7E,-7-7E,0 is an integral part of ribosome that also ta5es part in protein synthesis. ,bout =;O of cellular component of 7E, is ribosomal 7E, ts molecular mass varies from A/3/// to :.; million. TRANSFER RNA- Transfer 7E, -T-7E,0 acts as a carrier of amino acids. %ts molecules contains =;-=@ nucleotides and their molecular mass varies from ></// to >;///.Eear the middle of its molecule there is a se#uence of three bases called anticodon. These three bases are hydrogen bonded to a complimentary se#uence in m-7E, during protein synthesis.,ll t-7E, molecules have a L- shaped tertiary structure. The hydrophobic interactions are a maMor stabili!ing force in the tertiary structure of t-7E,. FUNCTION OF NUCLEIC ACIDS: - They have two important functions to perform---7eplication The genetic information for the cell is contained in the se#uence of the bases ,3 T3 +3 and C in the 6E, molecule. Ihen the cell divides3 6E, molecule replicates and ma5es exact copies of themselves so that daughter cell will have 6E, identical to that of the parent cell3 in this process the two strands of 6E, helix- unwinds and each strands serves as atemplate for the synthesis for a new stand. "ynthesis of proteins. This process involves Transcription and Translation Translation :- %n this step the double helix of 6E, opens up and two strands of 6E, acts as template for the synthesis of complementary 6E, molecule called messenger 7E, - m-7E,0 The following se#uences of bases in m-7E, formed and that of uncoiled strand of 6E, ta5es place )ncoiled strand of 6E, : C + , C T T , C C + T , , Tanscripted m-7E, :+ C ) + , , ) + + C,)) Translation:- 6uring translation3 m-7E, directs the protein synthesis in the cytoplasm of cell with the involvement of another type of 7E, molecule namely 3 transfer-7E, -t-7E,0 and the ribosomal particle. LIPIDS:- Lipids are waxy or oily substances which are present in all living organisms. Lipids are the constituents of all cell membranes. Lipids are esters of long chain fatty acids and alcohols. Lipids show some common characteristics Lipids are soluble in the organic solvents but insoluble in water ,ll lipids on hydrolysis give monocarboxylic acids - saturated or unsaturated0 Lipids may be broadly classified as "%'PL( L%P%6"- triglicerides0- Dats and oils Iaxes C&'PL(P -compound0 lipids-Phospholipids +lycolipids F')c#i$)s $7 %i/i!s To form a part of structure of biological membranes. Phospholipids serve as structural component of cell membrane To store energy for the cell. "imple lipids serve as energy reservoirs for animals "imple lipids act as shoc5 absorbers and heat insulators for the bodies of many organisms including humans. HARMONES- chemical compounds secreted by ductless glands which meditate communication between the cells and control various cellular activities are called as hormones.

ormones may be called as chemical messengers or chemical regulators. ormones are produced in ductless glands and transported by blood circulation to the target tissues for producing inhibitory or stimulatory effect. C%assi7ica#i$) $7 h$ .$)"s-$ased on chemical structures hormones fall in three categories"teroid hormones3 Polypeptide hormones3 ,mine hormones VITAMINES- , group of bio molecules which are not produced by the body but re#uired in very small #uantities for normal metabolic activities and healthy growth of human beings and animals are called as Vitamines. &n the basis of their solubility they can be classified intoI,T(7 "&L)$L( V%T,'%E("- Vitamines which dissolve in water are called as water soluble vitamins. (g. Vitamin $ and C &%L &7 D,T "&L)$L( V%T,'%E("- Vitamines which dissolve in oil or fat are called as fat or oil soluble vitamins. (g. ,3 63 ( and F. IMPORTANT NCERT 8UESTIONS Q: Ihat are reducing and non-reducing sugarsR Ihat is a structural feature characteri!ing reducing sugarR Q> Q< 6raw simple fischer proMections of 6 and L glucose. ,re these enantiomersR

Irite down the structures and the names of the products obtained when 6 glucose is treated with -a0 acetic anhydride -b0 hydrocynic acid3 -c0 bromine -d0 concentrated E& <3 -e0 %. QA (xplain mutarotation. (xplain its mechanism in 6 glucose.

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Ihat are essential and non essential amino acidsR +ive > eg. &f each. +ive reasons for the following-a0 amino acids have relatively higher melting point as compared to corresponding halo acids. -b0 &n electrolysis in acidic solutions amino acids migrate toward cathode whereas in al5aline solution these migrate towards anode. Q9 Ihat type of lin5ages are responsible for the formation of these -a0 G- elix formation -b0 H- sheet structure

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Ihat forces are responsible for the stability of G- helixR Ihy is it named as <.9 :< helixR Q@ Ihat is denaturation and renaturation of proteinsR

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Ihat products are obtained on complete hydrolysis of 6E,R Irite down the structures of purines and pyridimine bases present in 6E,. Ihat are complementary basesR 6raw structure to show hydrogen bonding between adenine and thymine bases present in 6E,. ow does 6E, replicateR +ive the mechanism of replication. ow is the process responsible for preservation of heredityR ,nswer the following about protein synthesis-a0 ow do 9A codons code for only >/ amino acids -b0 6uring translation which one of the two-end functional groups of the polypeptide is formed firstR Q:< Q:A ow are lipids classifiedR +ive an example of each class. ormones are chemical messengers . (xplain. Q:>

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Eame the deficiency diseases caused due to lac5 of Vitamin , 3 C3 ( 3 $ :3 $:>3 $93 and F. REDUCING ANS NON-REDUCING SUGARS :-

Those carbohydrates which contain a free aldehydic or a 5etonic group and reduce TollenJs reagent are called 7educing sugars. (.g. +lucose3 fructose3 galactose. &n the other hand which do not reduce TollenJs reagent and do not contain free aldehydic or a 5etonic group are called non-reducing sugars. (.g. 'altose3 Lactose3 "ucrose. Findly practice all the structures also.

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