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    Biomolecules Class 12 Chemistry Worksheet with detailed solutions

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    14. Biomolecules

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    Biomolecules Class 12 Chemistry Worksheet with detailed solutions

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    76 Ansichten23 Seiten

    Biomolecules

    Hochgeladen von

    Saksham
    Biomolecules Class 12 Chemistry Worksheet with detailed solutions

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    © All Rights Reserved
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    R. K. MALIK'S JEE (MAIN & ADV.), MEDICAL + BOARD, NEWTON CLASSES ‘ . — Enjoys unparalleled reputation for best results in terms of percentage selection www.newtonclasses.net BIOMOLECULES [DRILL ASSIGNMENT] CLASS — XII TARGET CBSE 1. Carbohydrates are usually defined as polyhydroxy aldehydes and ketones or substances that hydrolyze to yield polyhydroxy aldehydes and ketones. (a) Classification: They are classified on the basis of hydrolytic behavior as «= The simplest catbohydrates, those that cannot be hydrolyzed into simpler carbohydrates, are called monosaccharides. «The carbohydrates that undergo hydrolysis to produce only two molecules of monosaccharide ae called disaccharides; those that yield three molecules of monosaccharide are called trisaccharides, and s0 on. «Carbohydrates that hydrolyze to yield 2-10 molecules of monosaccharide are sometimes called oligosaccharides. {Carbohydrates that yield large number of molecules of monosaccharides (>10) are known as polysaccharides. Starch, rot 22 — (hon, buon boon buon comme Saatuesd—Genae ‘Thisindicates that glucose contains one primary alcaholc group. The primary alcoholic groupt-CH,OH) is avays present at the end ofthe carbon chain 1. Whatisan aldose, an aldotetrose,aketose, a ketohexose? Give an example ofeach, ‘Setution ‘Aldoses are monosaccharides that contain an aldehyde group. For example glucose. Aldotetroses are the monosaccharide aldoses that contain four catbon atoms For example, erythrase, Ketoses ae the monosaccharides that contain a keto group. Fr example, fructose. Ketohexoses are the monosaccharide ketoses that contain six carbon atoms, For example, fructose 2, What does it mean to say that D- and Lglyceraldehyde are enantiomers? Explain the meaning ofthe designations D and Las used to specify the configuration of carbohydrates, Solution 1D and L-lyceraldeyde are enantiomers, which means that two of these forms are non-superimposable miror images of each other. HO ‘CHO H—C—on buon Al the compounds which can be chemically correlated to isomer of glyceraldehyde are assigned D-configuation while those ‘which can be correlated to -) isomer of glyceraldeydeare assigned L-configuration, 23. Whatis the monosaccharide composition of sucrose, maltose, lactose, starch, cellulose and glycogen. Solution Te monosaccharide composition of the given carbohydrates Sucrose: 1 glucose and | fructose molecule Maltose:2 glucase molecules. Lactose: glucose and 1 galactose molecule ‘Starch: Long chains of many glucose molecules made and stored in plants and animals Cellulose: Long straight chains of many glucose molecules, also found in plants but wth diferent linkage ‘Glycogen: Highly branched chains of glucose molecules made and stored in animals and fungi but notin plants, 4 Use molecular structure to explain the following: (a) Fructoseisa ketone. {(b) Glucose san aldehyde. Solution (a) Since fructose contains C=O, that is, keto group in is Structure, means that itis a ketone and gives reactions of ketone. {b) Glucose contains ~CHO group, thai, aldehyde group in its structure. Ths indicates that tis an aldehyde andit also reacts with hydroxylamine to form an oxime, and adds a molecule of hydrogen cyanide to ferm cyanohytin. ‘5. Classify each monosaccharide terms of functional group and number of carbon atoms. Office.: 606 , 6" Floor, Hariom Tower, Circular Road, Ranchi-1, Ph.: 0651-2662623, 9636608812, 7546846949 8 R. K. MALIK’S NEWTON CLASSES @ % oH Hew ® ow “9 ol HOCH,CCH,OH HOCH, CHCHCHCHC—H_ HOCH;CCHCHCH;OH soe pA bu On ba on Sohn (a) Ketove(hetotriose) (b)_Addovealeherose) (c)Ketose etopentoe) (a) Keto tetrose) Draw al possible adoterotesand2ketopentotes Which aD and which te Lugar? Season 2epmnes oon oon Ho. ‘on wo A Lon — : " 4 bu ou bane nae pts | roy on e nton — H-ton WY OH HS OH cH:0H cH,0H OH O OH O Denthwose DThreose owhlse Shave 7. Which funetional group is oxidized when (a) D-gluconic acid and (b) D-glucuronic acd are produced from D-glucose? Solution (a) Carbonyl group is oxidized when D-gluconic acids produced from D-glucose () Hydroxyl aroup is oxidized when D-glucuronic acid is produced from D-glucose. |8. How does an c-anomeritfer froma f-anomer? Solution ‘Apa of stereoisomers that differ in configuration around Ci ate called anomers and the C1 carbon is called anomeric carbon, The {a and f- CoHOe + Cots Sucrowe Water, = «Glucose Fructose lelp= 2665 lalp= #525" alg 9 {b)_ Polypeptides are defined as along chain of amino acids joined by peptide bonds. They may be formed by partial hydrolysis of proteins or synthesized from fre amino acids, One end of every polypeptide, called the amino terminal or N-terminal, has free ‘amino group. The ather end, with its ree carboxyl group, is called the carboxyl terminal or C-terminal. 2. Name the products of hydrolysis of sucrose. Why is sucrose not a reducing sugar? (case 2010) Solution Hydrolysis of sucrose yelds glucose and fructose, Reducing capability Is defined by the presence offre aldehyde or ketone group. ‘The anomeric carbon of sucrose is not“free; since this carbon is used to link fructose and glucose together. The two hexoses in sucrose are joined trough a alycosidic linkage involving C1 of glucose and C2 of fuctose. Therefore this anomeric carbon cannot ‘open up the rng structure and react withthe reagent. Therefor, sucrose isnot reducing sugar. cH.0H CH,0H K ar) HAT Hone a H sorte | . on 5 7-0 on 4 on 4 (CH,0H of on AH oy cH,08 4 on ue 4 on tae ih a Dcxose BOFrucese Office.: 606 , 6” Floor, Hariom Tower, Circular Road, Ranchi-1, Ph.: 0861-2662623, 2635608812, 7546845949, BIOMOLECULES [DRILL ASSIGNMENT] CLASS ~ X11 u |. What s meant by reducing sugars? (csse 2010) Solution ‘reducing sugars a sugar which has 2 free aldehyde or ketonic group and is easly reduced by reducing agents. Carbohydrates ‘which reduce Tolens reagent or Fehling’ solution and have free aldehyde group are called reducing sugars. For example, actos, maltose, glucose fructose 4 Lstthe reactions of glucose which cannot be explained by its open-chan structure, (cBSE 2008) Solution ‘The open-chain structure of D (+)-glucose explains most ofits reactions, however, fails to explain the following fats (a) 0(¢)-alucose does not undergo certain reactions of aldehydes. For example, glucose does not frm 24-DNP derivative, and does not respond to Schif's reagent. {b)_ Glucose reacts with NH,OH to form an oxime, but glucose pentaacetate does not. {c)_ Glucose does not form the hydrogen sulphite addition product with NaHSOs, a), The process of mutarotation in glucose “Two cyte forms of glucose 5. How are carbohydrates classified? (ese 2007) Solution Carbohydrates are classified on the basis ofthe number of products formed on hydroyss. (a), Monosaccharides: These are the carbohydrates which cannot be hydrolyzed to simpler carbohydrates For example, glucose. (b) Oligosaccharides: These are the carbohydrates which on hydrolysis yield 2~10 molecules of monosaccharides. For example, (cl, Polysaccharides: These ae the carbohydrates which yield many molecules of monosaccharides on hydrolysis For example starch. ‘Additional Questions 1, Give one reaction to show the presence of ive hydroxyl groups in glucose. Solution ‘The reaction with acetic anhydride gives pentaacetate which confirms the presence of five “OH groups. SHO ge (Hort, + faHcono — HO COC, CH,0H cH,0cocH, ucose 2. How will you prove that all the carbon atoms of glucose ar in a straight chain? Solution ‘The reaction of glucose with HI gives n-hexane and it proves that all si carbon atoms are ina straight chain Ga (CHO), + HI > CHy—(CHi)q—CHs + CHy—CHI— (CH), CH ntenane Modohesane CH.0H Deucore Office.: 606 , 6" Floor, Hariom Tower, Circular Road, Ranchi-1, Ph.: 0651-2662623, 9636608812, 7546846949 2 R. K. MALIK'S NEWTON CLASSES. 3. Who proposed the open-chain structure of glucose? Draw this structure. Solution Bayer proposed the open- Cl 0g + C05 Sucre Ghcoue Fructoue 7. Which carbohydrates called grape sugar? Give its condensed structural formula Solution ‘Glucose i called grape sugar. Its condensed formula SHO (cHOM, cH,0H 8. Why cellulose in our diet not nourishing? Solution Cellulose in our det snot nourishing becausetisinsolubleand does not dissolve in water easily andsoitis non-digestible. Our body lacks the enzyme cellulose responsible for metabolizing cellulose. Office.: 606 , 6” Floor, Hariom Tower, Circular Road, Ranchi-1, Ph.: 0861-2662623, 2635608812, 7546845949, BIOMOLECULES [DRILL ASSIGNMENT] CLASS ~ X11 13 14.6TO 14.9 PROTEINS Conceptual Questions 1. Glycine exists 25a 2witterion but o- and p-aminobenzolc acids donot. Explain, Solution Inortho- end para-aminobenzolc acids, the lone pair of electrons on the NH, group is involved in resonance with the benzene sing, [Asa result acidic character of -COOH group and basic character of -NH, group decreases. Therefore, the weakly acidic~COOH group ‘cannot transfer an H* ion to the weakly basic “NH, group Thus, ortho-and para-aminebenzoic acids do not exist as zwiterions. NH in coon 00° too nn{_\—coon on wsi{ coo sion po wn a sowevern geno benzene ing is present. As ares ups scent ase and cepa proton om =COOM youp toroma swe, th—cH—COOH = Hyii—cH,—coo ore — 2. Canthe acd hoe fan amin ald be made by tenting th SOC Setuton nea bec the amin acco fomedin thei tp reas wth another melee tofor pepe aha and son N,CHRCOOH + SOC, > NH,CHRCOGL +50, «HC NH,CHRCOOH + NHCHRCOCL + HCl NHcHRCONMCHRCO 2. tea dt costing many fie an adequt et? Why or why nt? Solution No, diet consisting mainly of rice is not an adequate diet because I's deficient in iysine and threonine, which are essential amino acids required for growth and maintenance of health. Hence, their deficiency has to be supplemented by other protein-ich foods suchas pulses, ete 4. How many naturally occurring amino acids exist in proteins? How many ofthese ae synthesized by the bod? Solution “There are twenty naturally ocurting amine acids in proteins. Out of which ten are synthesized by the body. 5. State citferences between primary and secondary structure of proteins Solution Primary structure ofthe protein refers tothe covalent structure including the dsulphides bridges of each polypeptide chain. The conformation which the polypeptide chains assume asa result of hydrogen bonding is called the secondary structure. 6. Inthe dipeptide Gly-Ala, which amine acid has a free amino group and which has afree carboxyl group. Solution Glycine has free amino group, whereas alanine has afree carboxyl group. 2). The melting points and solubility in water of amino acids ae generally higher than that ofthe corresponding haloaids. Explain. (NCERT) Solution “The aminoacids exist as zwtterions. Due to this dipolar salt‘ke character they have strong dipole-dipole attractions or electrostatic attractions. Therefore. their melting points ae higher than the corresponding haloacids Due to salt-like character, their solubility in \ateris also higher than haloacids. |8, Where does the water present inthe egg go after boiling the egg? (wcerr) Solution When the eggs boiled, the proteins undergo denaturation followed by coagulation. The water present inthe egg gets absorbed! ‘adsorbed during coagulation. Office.: 606 , 6" Floor, Hariom Tower, Circular Road, Ranchi-1, Ph. 0661-2662623, 9836600012, 7546845949, W R. K. MALIK’S NEWTON CLASSE 9. Whatare essential and non-essential amino acids? Give two examples ofeach type. (wcerT) Solution ‘Amine acids which are needed for health and growth of human beings but are not synthesized by the human body ae called essen tial amine acids, For example, valine, leucine, et ids which are needed for health and growth of human beings and are synthesized by the human body ate called non sino acids, For example, glycine alanine, aspartic acid, et 10. Define the following as related to proteins) peptide linkage: (b) primary structure and (c) denaturation. (ncerT) Solution [a) Peptide linkage: A peptide bond is an amide linkage formed between -COOH group of one ceamino acid and NH, group of ‘the other amino acd by loss ofa molecule of water. @ i a I HCE BEB 04 C004 HNO HoH C0OH oH os xcne Aarne Peptide bond ty Ala) () Primary structure: The specific sequence in which the various c-amino acids presentin the protein are linked to one another Iscalled its primary structure, [e)Denaturation: When a protein in native form is subjected to physical changes such as change in ternperatue, pH, etc, the hydrogen bonds present in protein ae broken. As a result, unfolding of protein molecules occurs and the protein loses its bio logical activity. Thisoss of biological activity is called denaturation. During denaturation, the secondary and tertiary structures ‘of proteins are destroyed but primary structure remains intact. 111. What are the common types of secondary structure of proteins? (NCERT) Solution The conformation which the polypeptide chains assumes asa result of hydrogen bonding i called the secondary structure of the proteins. The two types of secondary structures are: helo and f pleated sheet structure +12, What type of bonding helps in stabilizing the a-helc structure of proteins? (weerr) Solution ‘The a-helix structure of proteins is stabilized by intramolecular hydrogen bonding between C=O of one amino acid residue andthe INH ofthe fourth amino acid esidue inthe chain 13, Differentiate between globular and fibrous proteins. (weer Solution Fibrous proteins consist of tinea treadslike molecules which tend tole side by side to form fibers. These serve as chief structural material for animal tissue. For example keratin in skin, al nails and woo) Globular proteins are those in which polypeptide chains folded around itself in such a way soasto give the entire protein molecule ‘an almost spheroidal shape. This lass of proteins includes al enzymes, hormones such as insulin fom pancreas, et. 114. How do you explain the amphoteric behavior of amino acids? (NcERT) Solution ‘Amino acids contain an acidic anda basic group inthe same molecule In aqueous solution, they neutralize each other. The carboxy group loses a proton while the amino group acceptsit As a resulta dipolar ion orzuiterion i formed. HaN—EH—cooH —>Hi—eH—COO™ R R Zoterion Inthe acidic medium, COO” of the zwitterion accepts a proton to form the cation (whereas inthe basic medium, NHS jon loves a proton to form the anion wlimorcoon Sine c00" So coo" R R R 0 2witeion a 3 Floor, Hariom Tower, Circular Road, Ranchi-1, Ph.: 0651-2562623, 9836608612, 7646846949 BIOMOLECULES [DRILL ASSIGNMENT] CLASS ~ X11 15 115, What sthe effec of denaturation on the structute of proteins? (NcERT) Solution During denaturation, the secondary and teniary structures of proteins are destroyed but primary structure remains intact. As 3 result of denaturation, the globular proteins ae converted into fibrous proteins and ther biological activity is lost. Textbook Exercises 1, Whatis the meaning ofthe a a itis used in a-amino acid? Draw a bond-ine structure showing the zwitterion form ofeach ofthe following amine acids: L-valine,L tryptophan, Lglutemine and -proline. Solution ‘The symbol a means that amino group I attached to the a-carbon atom. NH 1 COOH HiN—CH—COO HyNi— | wm de 00 O=C—NH, . | ‘Glutamine wie " ° & ee wie A Hit—Chy * naive I deci 2 Using three-letter abbreviations, identi all possible acyclic trpeptides containing Lleucine, L methionine and valine. Solution Leu-Val-Met;Leu-Met Val-LeU-Met;Val-Met-Leu; Met Leu Va 3, Three amino acids are combined to produce a tripeptide. 4 ° ° ° i. 1 1 is a k # 4 (a), How many peptide bonds does the tripeptide have? {b) Which amino acd residue is atthe N-terminal? {e) Which amino acd residue is atthe Cterminal? {@), How many different tripeptides could be produced using one of each amino acid? |e}, How many diferent tripeptides could be produced using one, two, or three ofeach amino acid? Solution (o) 2 (b) Firstaminoacid —_(¢)_Thirdamino acid 6 27 Office.: 606 , 6" Floor, Hariom Tower, Circular Road, Ranchi-1, Ph. 0661-2662623, 9836600012, 7546845949, 16 R. K. MALIK’S NEWTON CLASSES “4 Which specific class of bonds holds one amino acid residue to the next inthe primary structure ofa protein? Are these bonds covalent or non-covalent? Solution Peptide bonds hold one amino acid residue tothe next in the primary structure of a protein. These bonds are covalent. 5. Towhich functional groups from organic chemistry do peptide bonds belong? When a peptide bond is hydrolyzed, which two func- tlonal groups are produced? Solution Peptide bonds belong to amide funcional group. When 2 peptide bond is hydrolyze, carboxylic acd group and amine group are produced. {6 List the chemical bonds or forces that are primarly responsible for maintaining the (a) primary: (b) secondary; () tertiary and (d) quarternary structures ofa protein. Solution (a). Peptide bond (} Hydrogen bond {e)_ van der Waals forces, disulphide bonds, hydrogen bonds, electrostatic interaction (Hydrogen bonds, van der Waals forces, electrostatic interaction. 7. Examine the a-heli conformation, Are amino acid side chains aranged all inside the hel all utsie the helix or randomly? Solution ‘Amino acid side chains are arranged outside of the helix. Previous Years CBSE Questions 1. What are essential and non-essential amino acidsin human food? Give one example of each type. (case 2010) Solution “The essential amino acids are those which must be obtained from food sources. These cannot be synthesized by the body insufficient {quantities to satisfy the nutritional requirements for good health, and thus must be Included inthe diet. For example, leucine, Isoleu- Cine, valine, lysine, threonine, tryptophan, methionine, phenylalanine and histidine (On the other hand, non essential amino aids can be synthesized by the body from other amino aids For example, arginine, alanine, asparagine, aspartic aid cysteine, glutamine, glutamic acid glycine, proline, serine, and tyrosine, 2 Amino acids maybe acidic, alkaline or neutral, How does this happen? (esse 2010) Solution ‘Acidic amino aids contain more numberof carboxyl groups than amino groups. Basic amino acids contain more number of amino groups than carboxy groups. "Neutral amino acids contain equal number of amino acids and carboxyl groups. 3. Explain whats meant by (a) peptide linkage and (b) glycosidic inkage. (cBse 2009) Solution (2) A peptide linkage is an amide bond formed between-COOH of one amino acid and -NH, group of another amino acid by the loss of water molecule HCOOH HG cOOH > Mc EDE-cH-—cOOH chy Loa Peptide linkage (6) Linkage formed between two monosaccharides units through O atom i called glycosidic linkage. Office.: 606 , 6” Floor, Hariom Tower, Circular Road, Ranchi-1, Ph.: 0861-2662623, 2635608812, 7546845949, BIOMOLECULES [DRILL ASSIGNMENT] CLASS ~ XI 7 Define the term denaturation in relation to proteins. (€BSE 2008), Solution ‘The structure ofa protein is essential to its activity. When a protein s subjected to physical change (suchas change in temperature) lorchemical change (such as change in pH it loses its biological activity. Tiss called denaturation of prateln. Additional Questions 1 Write the name and the structure of the simplest amino acid which can show optical activity Solution ‘Alanine the simplest amino aid which can show optical activity. Han coon Hy 2 itive the structure of zwitterion formed from alanine Solution Wi GH=COOH WG COO Hs cy Nanine 2witeron of alanine 3 ustrate AlaGly. Phe tripeptide, Solution i I Ha —GH CNH —CHy CNC COOH cy CHGHs a Os ts anime Gydne Phenylalanine ‘4. Name the derivative ofa dipeptide used as a sugar substitute Solution Aspartame s the derivative of dipeptide used asa sugar substitute. 5. What type of bonds are responsible for secondary structure of proteins? Solution Hydrogen bonds are responsible forthe secondary structure of proteins 6. What does 3.6, stand forin 3.6}, arhelie? Solution 3543 Indicates that each tum ofthe helbc has approximately 3-6 amino acids and a 13-member ing is formed by the hydrogen bonding. 7. Give an example of reversible protein denaturation. Solution “The coagulation of egg white on boing of eg9 protein isan example of irreversible protein denaturation, |. Which bonds in the backbone of peptide can rotate freely and which cannot? Give reasons. Solution “Thefree rotation of peptide chain can only occur around the bonds joining the nearly planar amide groups tothe a-carbons.The ree rotation about the peptide bond is restricted due to the partial double bond character of the C-N bond in the peptide linkage. “Therefore, “CONH- group is planar and rigid Distinguish between intermolecular and intramolecular hydrogen bonding between the backbone group on polypeptide chains. In what typeof secondary structure do you find intermolecualr hydrogen bonds? In what type do you ind intramolecular hydrogen bonding? Solution Secondary structure arises from hydrogen bonding along a polypeptide backbone, Office.: 606 , 6" Floor, Hariom Tower, Circular Road, Ranchi-1, Ph. 0661-2662623, 9836600012, 7546845949, Is R. K. MALIK’S NEWTON CLASSES {a} The intramolecular hydrogen bonding occurs between peptide units ofthe same chain. This type of bonding requires the pep: tide backbone to be 30 and not plana. Te avoid bond angle distortions, the fist C=O of one amino acid forms hydrogen bonds With the NH of the third amino acd, resulting in a colled arrangement called a-hels (b)Tominimize steric interaction between bulky alky group, the peptide backbone twists in such a way that the alkyl group rotate away from each other. This deviation from planar structure results in formation of pleated sheet structure, Ths arrangement i

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