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GATE Life Sciences (XL)2010 Save paper… Save trees… For more Questions and Resources for your CSIR/ICMR/DBT/ICAR/GATE/UGC/JRF NET Life Science Examination please visit: www.easybiologyclass.com 1 GATE Life Sciences (XL) 2010 (Graduate Aptitude Test in Engineering: Original Question Paper) Biochemistry (I) Optional Paper Questions 1 – 10 carries 1 mark each: 1. Nucleolus is involved in the synthesis of: a. rRNA b. tRNA c. DNA d. mRNA 2. In tryptophan operon, tryptophan acts as: a. Repressor b. Activator c. Co‐repressor d. Co‐activator 3. Positive selection of T cells ensures: a. MHC restriction b. Self‐tolerance c. TCR engagements d. Activation by co‐stimulatory signals 4. A DNA binding motif is: a. Helix‐loop‐helix b. Helix‐turn‐helix c. Helical wheel d. Loop‐helix‐loop 5. Amino acids responsible for N‐linked and O‐linked glycosylation of proteins are: a. Asparagine and Aspartic acid b. Glutamine and Serine c. Glutamic acid and Serine d. Asparagine and Threonine 6. One of the following compounds is NOT a neurotransmitter: a. Dopamine b. Glutamic acid c. Histidine d. Glycine 7. Approximate molecular weight (kDa) of the product after translation of a 390 base mRNA will be: www.easybiologyclass.com

GATE Life Sciences XL 2010 Part 3 Biochemistry (I) Optional Paper by Easybiologyclass

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Page 1: GATE Life Sciences XL 2010 Part 3 Biochemistry (I) Optional Paper by Easybiologyclass

GATELifeSciences(XL)‐2010 Savepaper…Savetrees…

FormoreQuestionsandResourcesforyourCSIR/ICMR/DBT/ICAR/GATE/UGC/JRFNETLifeScienceExaminationpleasevisit:

www.easybiologyclass.com 1

GATELifeSciences(XL)2010(GraduateAptitudeTestinEngineering:OriginalQuestionPaper)

Biochemistry(I)OptionalPaper

Questions1–10carries1markeach:

1. Nucleolusisinvolvedinthesynthesisof:a. rRNAb. tRNAc. DNAd. mRNA

2. Intryptophanoperon,tryptophanactsas:a. Repressorb. Activatorc. Co‐repressord. Co‐activator

3. PositiveselectionofTcellsensures:a. MHCrestrictionb. Self‐tolerancec. TCRengagementsd. Activationbyco‐stimulatorysignals

4. ADNAbindingmotifis:a. Helix‐loop‐helixb. Helix‐turn‐helixc. Helicalwheeld. Loop‐helix‐loop

5. AminoacidsresponsibleforN‐linkedandO‐linkedglycosylationofproteinsare:a. AsparagineandAsparticacidb. GlutamineandSerinec. GlutamicacidandSerined. AsparagineandThreonine

6. OneofthefollowingcompoundsisNOTaneurotransmitter:a. Dopamineb. Glutamicacidc. Histidined. Glycine

7. Approximatemolecularweight(kDa)oftheproductaftertranslationofa390basemRNAwillbe:www.ea

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Page 2: GATE Life Sciences XL 2010 Part 3 Biochemistry (I) Optional Paper by Easybiologyclass

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a. 48b. 26c. 39d. 14

8. Lineweaver‐Burkplotisaplotof:

9. Amixtureofproteins(W,X,Y,Z)eluteformSephadexG‐200columnintheorderW,

X,Y,Z.TheproteinwithmaximumelectrophoreticmobilityonSDS‐PAGEwillbea. Wb. Xc. Yd. Z

10. Specificprecursorofallprostaglandinsis:a. Oleicacidb. Arachidonicacidc. Palmiticacidd. Α‐linolenicacid

Questions11–20carrytwomarkseach

11. Chymotrypsinandlysozymeareinvolvedrespectivelyin:P.RemovalofsuccessivecarboxylterminalresiduesQ.HydrolyticcleavageofpeptidebondR.CleavageofglycosidicC‐ObondS.Oxygentransportinblood

a. P,Qb. Q,Rc. Q,Sd. R,S

12. MatchtheitemsinGroupIwiththoseinGroup2GroupI GroupIIP.Isotypeswitching 1.VHdomainQ.Clonalanergy 2.Non‐responsivetoself‐antigenR.ClassIIMHC 3.Non‐responsiveTHcellsS.Self‐tolerance 4.β2‐microglobulin

a. P–1,Q–4,R–3,S–2www.easy

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b. P–2,Q–4,R–1,S–3c. P–1,Q–3,R–4,S–2d. P–2,Q–1,R–3,S–4

13. MultipleRNApolymerasetranscribesaDNAtemplate,unwindingabout1.5turnsofDNAtemplatepertranscriptionbubble.FromthestructuralinformationofclassicalB‐DNA, how many transcription bubbles are possible for a 180 base pair DNAmolecule?

a. 12b. 27c. 6d. 270

14. MatchtheitemsinGroupIwithmostappropriateseparationtechniqueinGroupIIGroupI GroupIIP.Mixtureofglycineandalbumin 1.GaschromatographyQ.Mixtureof20and60kDaproteins 2.DialysisR.Histonesfromnuclearextract 3.AffinitychromatographyS.Lectins 4.Sizeexclusionchromatography 5.Thinlayerchromatography 6.Cationexchangechromatography

a. P–1,Q–4,R–3,S–5b. P–5,Q–3,R–6,S‐1c. P–2,Q–4,R–6,S‐3d. P–6,Q–5,R–2,S–4

15. Inthetwohalfreactions:Acetaldehyde+2H++2e‐→Ethanol ∆Eo=‐0.16VNAD+H+→NAD++2H++2e‐ ∆Eo=‐0.32V(F=23,063cal/V)The∆Goforthecoupledreactionwillbe:

a. +7400calb. ‐7400calc. ‐22200cald. +22200cal

16. MatchtheparametersinGroupIwiththecorrectoptioninGroup2GroupI Group2P.Km 1.CatalyticefficiencyoftheenzymeQ.Kcat/Km 2.AffinityofenzymetotheinhibitorR.pKa 3.AffinityofenzymetothesubstrateS.K1 4.Maximumbufferingcapacitywww.ea

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a. P–3,Q–1,R–2,S‐4b. P–3,Q–1,R–4,S‐2c. P–1,Q–2,R–4,S‐3d. P–1,Q–4,R–2,S‐3

17. Theriseperresidueofα‐helixisabout1.5Å.Aproteinspans2nmbilayer,7timesthrough its trans‐membrane α‐helical domain. Approximately, how many aminoacidresiduesconstitutethetrans‐membranedomainoftheprotein.

a. 105b. 450c. 30d. 190

18. MatchtheproteininGroupIwiththeircorrectfunctioninGroup2GroupI GroupIIP.Shakerprotein 1.InnermembranereceptorQ.Bacteriorhodopsin 2.ActivetransportR.Porin 3.VoltagegatedK+channelS.ABCtransporter 4.LightdrivenH+pump 5.Membranefusion 6.β‐barrelsimplediffusionchannel

a. P–4,Q–2,R–3,S–5b. P–5,Q–3,R–4,S–6c. P–6,Q–1,R–5,S–4d. P–3,Q–4,R–6,S–2

19. Themetabolicdisorders,alkaptonuriaandphenylketonuriaarecausedbydefectsintheenzymes:P.Glucose‐6‐phosphateQ.PhenylalaninehydroxylaseHomogentisate1,2‐dioxygenaseS.Tyrosinase

a. Q,Rb. P,Rc. P,Qd. Q,S

20. MatchthemetabolicpathwaysinGroupIwithcorrespondingenzymesinGroupIIGroupI GroupIIP.β‐oxidation 1.RibulosebisphosphatecarboxylaseQ.Glyclysis 2.Phosphofructokinase1www.ea

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R.Gluconeogenesis 3.PhosphoenolpyruvatecarboxykinaseS.Calvincycle 4.Thiolase 5.Phosphofructokinase2

a. P–4,Q–2,R–3,S–5b. P–3,Q–2,R–4,S–1c. P–3,Q–1,R–5,S–2d. P–4,Q–2,R–3,S–1

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