Exam II Fall 09

Exam II Fall 09 - 3 C HEM 4S-$1 h*iochernistry E xan $(D 1...

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CHEM 34S-$1 *iochernistry h Exan: ? $ - Octohrer 21,20A9 ; (D Part l: Multiple Choice 12 ptt. eachl 1 far questians 1-35, r&r:ose th* single &*sl answei' for earh Euestion ar prabl*m. Thi: pratein has multiple ccnfcrrnati*r'u &at are fr:lly aetive. This e*zy:Tre requires a c*tactor t* be fully active. This anzyme is capable of re.ad*pting its natlve confcrrnrati*n outside tl're cell. Inside rhe cell, this enzyrne needs a chaperone to lold properly ff Wnicn of the C*llowing is not a condiiion that is kncwn fo fause prot€in denaturation? @r*rr*n el-v high concentrations cf protein^ -6 Very high 0r very low pll. ci [levated temperatures. il The pre*e*ce of *rganle s*Xvet:tr. Y Anenzyrne wa* extracted frorrr ir: c*ltular environment, purifled and tested feir activity and f*und ts be aetive. The purified artive enzym* was then denatured using urea. When the urea uras reitl*ved the pr*tein was fouxd to be fully active again. Based on this infermation alcne, what can be said abnut this prerteinl S Wtricir of the iollowing is an example of protein denaturation? @.1: The solidifuing eg[ rvhites upon heating. *tr The brorvning of red meat from age. ft in* r*i**ni*fof muscles in deadTiodies. dl The tighteniig up af ioint* as c:n* *ges. ,::: q{ wt;*f, of the follo,.ving intrinsic trarts cf henroglobin would not be affecred by its denaturation? lts UV ahsorption propert;es. @ rt* moleculai weignt.' c) lts a-helical content. t)t lts oxvgen transport capabilities. .S}"" Acccrding tri the rnolten glcbule rnodel *f prot*in fntrding: aj rfue p*lvpeptide chain farrnrs fslcal 2o structures flrst bef$re co$tact between 2o structures occurs. b) protein folding is a randomizerl, verv slow preicess. if,e polypepti#e chaln ccllapses in{o a u'loose" 30 slru$rsrethat is sirnilar t* its final strufrure" -dr the folding process is not driven by hydrophoi:ic interactions. 'd tl',e binding of hvo different lrgands to one protein was tested and it was tound that ligand A baund more tightly ro [he pr*tein than ligand 6. An*ther way of repsffins this cbservation w*uld tre rc state,t]rat tlre Q o{ the ,ffitein fcr ligand A is -- the lQ of the prstein for ligand B' (@/r fess than b) greater c) equal to dl denendenl an H :t
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The ei6ht stfitelnenis below ar* ccnclusionr that may or rney nof be drarvn from tl^re ftNAse fcrlding experirnent Whieh of the c*nclusinns ar€ $upport*d by the experi*rental regults? i lt proteln f*ldtng occurs in a ranelorn and unpredictalile way. cy. iii on* potrypeptldE chain ca* *dapt severa? eonfermatisrls and rernain funetional. 1 ,Q the infbrmation for a protein's tolded structure is in its primary structure (fr-UP protein bl.di*F canno.t be a random.ized process. q ul , the potential for forming multiple disulfide bonds in a protein often results in mis-folding ( JF a potypeptide cloes not necessarily have to be synthesized in the cell in order to fold praperty and harn v -" tunctionality as a proterin "\ uiil reducing agents aie requirerl for alI proteins ta fold properly. G. ryi"liltional mis*pairing of cystqr.ne" residues rcausing incorrect disulfide bonds) can be conected by ad<.Iing
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Exam II Fall 09 - 3 C HEM 4S-$1 h*iochernistry E xan $(D 1...

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