|. All proteins contain the (A) Some 20amino acids [B)_Dillerentomina oxide (C200 Amino acidecccurrng i nats [D}_ Only @ fow amino acide Proteins contain (A) Only t-omino acids [B}. Only Domine ace IG) DtAninoadide [D) Bath (A) ond (8) The optically inactive amino acd is (A) Glycre (B) Some (G) Theosine (0) Vatinn At neutral pH, a mixture of amino acids in sohtion would be predominantly: (A) Dipolorions (2). Nonpolarmolecues G) Paste ond manovalent [D) Hydeaphabie The true stotement about solutions of enna acide ot physiological pH ix (A) All anine acids cortain bath postive and negative chages 1) Alonve acs concin poste chagod (G) Some amino acids contain only postive charge [D}. All omiro acids comin negatvaly charged ‘dochoine PH (isoelectricpH) of alanine is (a 0.02 Boe 6s p72 ‘Since the pK values for aspartic acd are 30; 019 bd 100, 0 felows nat the inaelacre (Hie Wao Bae aso P60 ‘Sulphur containing emine ocid is (A Methionine} Leucine (Q. Nalne P) Asparagine ‘An example of sulphur containing amino Sager & sphur containing [AL Amine mercoplopropanci acid [B} 2Anincdnethylbvanaic acid [G) 2-Amina 2 dycmnypropanaic cid [D), Amino cea acid . All the following are sulphur containing ‘amino ocids found in proteins except (A Cyasine BB} Cyne (Q Metiorine 1D} Thorne + An erematic amine ectd is (A sire 1B) Tyrone [Q Tawrne P) Arginine2 13, 4. 15. 16. wv. w. The functions of plasma albumin are A) Osmosi B) Trompe (©) Immuniy ———_—B} both (Aon (8 ‘Amino acid with side chain containing bbasie groups is (A). 2AminoS quonidovaleric acd (8) 2?yraisin carbonic oid [CQ] 2Amino’:mereaplepropanoicacid (0) 2minoprepancicacis ‘An exemple of a-amino acid not present in proteins but essential in mammatin sotabotiarnia [A] Amino dhonypropancic ccd (8) 2Aminedhydronplutncic ood (C) 2Aminn .mercoplcbutonie cel (0). 2Amino’Lmercaplopopanaic acid An essential amine ecid in man is (A) Aspanate Bh) These (C] Mobiorie —B} Serine Non essential amino acids [A]. Are not componentsftiesve pomins (6), Maybe sntesizedin the body from essen ‘omine oade a D Have nara inthe metabolism ‘May be eynthasized inthe body in diseased stot Which one of the following is semi- ‘essential amino acid for humans? (A) Valine B) Aginine 1G bysine [D) Tyrosine An example of polar amine acd is 1) Alonine (8) lovcine 1G Aginine (0) Yale ‘The amino acid with anonpelar side chain is WA) Seine (8) Yotine [G) Asperagine —(D} Thrscnine Aketegenic amine odd 1) Valine (8) Gyekine (Q leucine (0) Thesnire a. ‘An amino acid that does not form an o- hholix (A) Vatne (8) Fine (G) Iyosne 1D) byploptan ‘An amino acid not found in proteins is (A) BAlorine 8) Foie (G) lyine 1D) Fistine In mammalian tissues serine con be @ biosynthetic precursor of (A) Mahoning (8) Gycine (2) Tryptophan (0) Phenylalanine Avdcerbespiaoh ofetinbwece” (A) Agiine (8) Asparicacd (Gone (0) Hine Bluret eectionis spot er (A) -CONnges 8) -CSNH, group 1G =DeANe, goup[O} Alfihse Sakaguchi’s reactionis specific for (A) Tyosine (8) Proline (9 Aginine (D) Cystine Million-Nasse’s reaction is specificfor the ‘amino acid: (4) Typlophan (8) Tyrosine [G) Phenylalains —[D} Arginine Ninhydrin with evolution of CO, forms.a blue complex with (A) Peptide bond (G)Seworin [B) o-Amino acids [D) Histamine The most of the ultraviolet absorption of proteins above 240 nm is due to their Content of 1A) Teyptoshan (8) Assorote (9 Ghomaie ——_[) Alenine Which ofthe followings a dipeptide? (4) Arsire (8) Glaatione (Glucagon) BLipeprosin Which ofthe following i 2 hipeptide? (A) Amerie (8) Onpcin (C Glvatione (0) Kalina. A peptide which acts os potent smooth ‘muscle hypotensive agents, (A Glwshione Brodin (Q Tryecidine——B} Gromicdins ‘A tripeptide functioring as an important ‘reducing agent in the tissues is (A Brodin 8) Kolin (Q. Trositin P) Gluothione ‘An example of metalloprotein is A Cossin 88) Conolasnin (Geli P) Sdiine . Corbonie anhydrase is en exemple of A Upopratsin 8) Phezphoprotin (A) Motllopretin )_ Chromeprsin ‘An example of chromoprotetn is (A) Hemoglebin ——B) Sane G Necein P} Ghudin An example of sceroprotein is (A Zein BB) Kerain (C) Gutenin } Oreglobutn Casein, the mill protein is {A Nucboprotein (8) Chromerrosin (G Phoshoprosin 2) Gycopeten ‘An example f phosphoprotein present in ogg yolk is 1A) Oveobumin 8) Ovegabuin (G Overisin §—) Avid ‘A simple protein found in the rucleopre- teins of the sperms A) Frlemive (G. Gaaln BB) Protamine P) Giebulin Histenes ore A Honicate protamine [B)_Prokinsrichin ysiraand crgiine (Q_ Froteinswit high moleculcr weight [D}_ Insoluble in water end vary dite aces The protein present in hair is (A) erin BB) Blstin [G) Myosin 1D) Teopocallgen 51 The amino acid from which synthesis of the protein of hair keratin takes place is (A) Alanine (8) Methicnine (9) Proine (0) Hydroxypotine In one molecule of albumin the number ‘of amino ocids is (4 510 (8) 590 9 610 (0) 650 Plasma proteins which contain more than A hexosamine are (A) Micogebuins (8) Gheoprtens (Q. Mucoprtsins (D) Onsomucoids After releasing 0, at the tissues, hhomoglobin transports (A) COs ard protens the lungs 18) 0, he lings (9) COjard protonstothetisve (0) Notions Etlers-Danlos syndrom characterized by hhypermobilejoin's and skin abnarmaliios sve 1 (A). Abromalty ingore er procollagen (0) Defectoncy oly oxidase (9. Deticiony of pchythydrowose (0) Debciony of hay hycronfase Proteins are soluble in (A) Anlycrousacetonel6) Aqueous clechol (9) Anhydrous alohol(O) Benzene ‘A corecl protein soluble in 70% alcohol ‘bur insoluble in water or salt solution is 4) Glvetn (2) Albomin (8) Protamine [D) Gian ‘Many globular proteins are stable in solution inspite they leck in (A) Disslphide bonds (8) Hydrogen bonds (G Salrbods ——[D} Non polar bonds The hydrogen bonds between peptide Inkeges of eproten molecules aretnter fored by (8) Goonitina (9) Ovaicacid [B) Uiccxid [D) Saleyic acid52, lcbuler preninshovecompleay folded ‘hein and the axel Fett tie leneth te brow is [AL tessthon 10 and generally not great than ne (8). Generally 10 [Q) Gracie: thon 10 and generally 20 [D) Greater then 10 53. Fibrous proteins have axial ratio (A) tessthen 19 (8). Leeethon 10 aad general not great han He (9) Gereraly 10 (Greater then 19 54, Each turn of a-helix contains the amino ‘acid residues (number 36 8) 30 19 42 (0) 45 55. Distance traveled per turn of auhelix in (4) 053 054 1G 04a 1p 0.8 56. Along the orholix each amine acid residue ‘advances in am by (4) 015 1 G10 IG 012 (p 020 57. The number of helices present in a collagen moleculeis a 2 a3 me In proteins the e-helixand p-ploated shoot ‘are examples of (A) Prmary erect (6) Secondry arvcure [G) Tetarysrucnre (0) Quowmarysrvcure 59. The cholix of proteins is (A) A pleated srectire [B) Made periodic by deulphide bridges IG) Anorpetiodestucere [D) Stabilsed by hydrogen bonds banween NIL tard CO grup af he mainchoin a. ‘At the lowest energy level a-helix of polypeptide chain i stabilised 1A). By hydragen bonds rmad bohvoon the Ho peptide Nand the carbon O ofthe residue [B}_Disulpice bonds [G) Non poler bonds [D)} Ester bonds Both e+helix and f-pleated shoot confor: ‘mation of proteins were proposed by (A) Wotton ond Crick [B) Paving ond Comy [G) Waugh end King [D} ¥S.Ro0 The primary structure of fibroin, the principal protein of silk worm fibres Consists almost entirely of 14) Sich (8) Aspartate 1G) Keron [P) ypophon Tertiory structure of a protein describes (A) There 0! oninoocids (8) locaton of diphide bonds [G) lopresionsofprasire (0) The maysot prt fading Inaproteinmolecule the disulphide bond isnot broken by (A) educon (8) Oxdaten {9 Denawraton (0) Heardifrenton ‘The technique for purification of proteins that cam be made specific for given protein is (A) Galion chomotography (8) lonexctangechronatarophy (G) ecropiorsis (O}_Afiriy chrometography Denoturation of proteins results in (A) isrpionct primary sete (8) Breckdownaf peptde bords {G)Destucton af ydroges bends (D) troversisle changer inthe mobula67. Ceruloplasmin is WW) aygbbuin (8) aglcbulin 10) fialabuin 10} Nore of these The lipoprotein with the fastest electro phoretic rrabiity ond the lowest traghye- je content ie WA) Chlonican 8) MOL KF) (9) rox 69. Thelipoprotein associated with orf vation of LCATis Ws) How (@) OL i) ve to) oe 70. Theapolipoproten which act a: activator of tcarie 1) Al B) AW F) ca ig 0 71. The epolpeprotein which oxts at ectator Theses 1) Apow B) Aeo8 F) Apc 19} Apo 72. The apolipoprotein which forms the ‘component of dhylomicron ie 1) 8100 a) 4a re jo ‘The apolipoprotein which from the integral component of VIDLis a) sac (9) 48 ma (0 7a, ‘The apolipoprotein which sets as ligand forLDL receptors Ww) B48 (8) 8160 ra ime 75. Serum LDL has been found te be increased A) Chsructhe javelin BB) Hepctic aundice I) Hemalyicjaundice Bi) Malabsorption sydme oprotein associated with ence of coronary wm (8) MOL KE) 10) Ho 7. 78. BI. A lipoprotein inversely related to the incidence of coranary artherosderosis is wa) vine B) me re) we P) Hoe The primary biochemical lesion in ho- mozygote with familial hypercholester- olemia (type tha) is JA) Loss of feed back inhibition of HG redutaue B) Lasse apdiponmnin & {C) increased production af LLfram WUDL B) Fanctonal deficiency of plasma membre receptors forLOk In abetalip oproteinemia, the biothemical defectisin (A) Apa aynbesis B) Uppratealipase octiay KE) Cholesarales te hyceclase Bi) LEAT octay Familial hypertriaacylalyceralemia is associated with A) Orerprodoetion af IDL B) lrcreared LD concentration KE) Incroased HO concermation PB) Sowclecronce of chylomicrons For synthesis of prostaglandins, the essential fatty acids give rise to a fatty acid containing A) 12 carboactoms 8) 18 carbon cfoms KC) 20 carbon toms |) 24 corbon crams All active prostaglandins have at leastone: double bond betwreen pasifions A) Panda B) 10and 11 I) Wand14 Bh) Iéand 17 A) 02-06mmd/ fi) 0.9-2.0 mmol/L KE) 185demdf P) 2.65.demoyL HDL, have the density in the range of JA) 1.008.019 B) 1.019-1.02 IE) 1:09241.089 fp) 1.089-1.12590 veproteins have the density in the 92 of WA) 0.95-1.008 a) 1.001015 Ie) 1019-1.089 fo} 1.089-1.125 IDL hawe the density in the range of WX) 095-1.008 a} 1.051018 Ke) 1.019-1.092, (0) 1.092-1.188 Aspitin inhibits theacivity of the enzyme: WA) Upcnygenase 8 Cyddoopgenase KE) Prasobdipae A, [D) Phasohalnase Ay A suicide enzyme’ is WX) Cydanigenase (8) bpaongenate I) Prombipme A, 10} Frosohoinase A, darecte WA) Upogeresis |B pas IE) Gleanengenenis |B} Giycogenaiyis ‘The optimal pH for the enayene pepsin is fk) 19-20 1) 52.080 a) 405.0 i) 5.002 9s wy) Ha (Bh Bie sas Ke) can {0} Erealeinase ‘The optimal pH for the enayme rennin is ww) 20 (81 40 K) 80 (60 ‘The optimal pH for the enayme trypsin is i) 10-20 (1 204.0 K) 52-42 1) 5.06.2 ‘The optimal pH for the enzyme chymo- teypain ie Wy 20 (8) 40 K) 60 1 80 Trypsinogan ie converted te ative trypsin Y WA) Erterckinase Ky na (8) Bile sats 10) ey Pepsin acts on denatured proteins te produce |) Protecses ard pepo nes B) Paoypegicies FE) Peptides BP) Oipepsdes 97, Renin converts casein to paracassin in Prosonce of WW) Cav B) Mgr KE) Ne BK 98. An expopeptidaseis 1) Tamsin B) Chrmoryasn FE) Blazase P) Eesme 99, Theensyme trypsinis specific for peptide bends of N) Basic amine acids BB) Acdicamina acds IE) Ammaticaminaacds Bi) Nestta small amino acid residues (A). Unchorged amina acid residues Bh) Asdicaminn ands FE) Basic amino ocid P) Small aminoacid msider OL. The end product af pratein digestion in Gini: WN) Opeptce B) Tepeptide F) Poyperde —) Ameaacd Notural isomers of amino adds ore absorbed from intestine by (A) Pasivedifision 8) Simpledifusion FE) Faciiced dition) Acive process Abnormalities of blood clotting are A) Hoonophlia —B) Chrismmandisease F) Gow P) Boa fa ond (8) ‘Ap important reaction for the synthesis of amino acid fram carbohydrate intermediates is transamination which 102, 103, os, requires the cofader 8) Thonn B) Ribatovn FF) Nace DP) Pydoxa phosphine