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BIS102 Hilt W07 MT2

BIS102 Hilt W07 MT2 - lof3 BIS 102 Name_g Winter 2007 Last...

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Unformatted text preview: lof3 BIS 102 Name___g%_________, Winter, 2007 Last First K. Hilt Second Midterm Score (100): R—group pKa’s: D (3.9), E (4.2); H (6.0); K (10.5), R (12.5); C (8.3); Y (10.1) The following are true/false questions. Each question is worth 5 points: 1 point for choosing the correct “T” or “F”, 4 points for correctly defending your answer. 1. F The most important weak bond for determining stability in 2°, 3°, and 4° protein structure is the hydrophobic effect. ‘. in 2°. H—biafA. awe Hm, M W +1 2. F Reverse turns are stabilized by a single H-bond, between the R-groups of the first and third amino acid residues that com rise the turn. +1 HAMAL WW a: firm; 4% NAM M :+ is neat M Ma. 10c 3r0wgs. *1 3. ‘T Proline is rarely found in (Jr-helices and [El-pleated sheets. prohm W m... rm 3am“ 16w bow. A460 tam 4M1. +341 new 431v “Jame. 4. F The peptide sequence TEDIIEIéV might form an a-helix at pH 1. +/+ rwnflgm rt. K M H Sik Janina w'uvu cm +0.4... + 2., 4” '2— 5. F Deoxyhemoglobin predominantly contains iron atoms in the hemes that are in the low a ‘ ‘ ‘ . m Now M Mt ‘m Hub \M‘jm SQ‘W $77M. ’Bméimj 4 0; \5 reavfiv-ei +0 amvevi- -\-o HA2, \M 56mm .(_,,(-M_ +2: 6. F Binding of a chloride ion to hemoglobin creates a single salt bridge to a histidine and results in the pKa of the histidine being lower. +1 B law. 5‘, or ‘ i \ ‘ * .— N’W ‘ Q a \ *l D“. “(-994m5‘ Elm *— C1. 7. F The pKa of a lysine residue in a protein increases substantially when an arginine side chain in the same protein comes into close proximi . u u ‘H \ “fin”. 519.1 mm \g-wflgi 10:1" “0" + “'31-. NM— stgez Q K4. . +z~ 8. F The peptide sequence VEGCYALM is an internal sequence, most likely derived by f, :jtlawwcyib sihefiKMK.Tk-Lolrm 3M L‘ M—fa/QMWWCJWW Biological Sciences 102 9. 10. 11. 12. 13. 14. %OzBound 886883888 20f3 Name % F 0.010 moles of 02 will be bound if a liter of blood containing 45 g of hemoglobin is transferred from 20 torr, pH 7.2 to 60 torr, pH 7.6? Hemoglobin has a molecular weight of 68,000. Show all calculations. +4 (mblS’xlll‘lMQ "Ha “Ma %)(4l = 2.1247 “Band 0. bImUnj sue/A. H F The amino acid residue at the N—terminus of a peptide is lysine. When this residue is labeled with the Edman reagent and eluted out of the column in the protein sequenator, the peak will come out near the beginning of the elution. +1 \ m bisfiQTl-lv Ii wnl be, m Ljawofm...’ .1224 +1, +4.; +ura—‘ _ ‘ wwi‘Kmsi‘lzC/Ltw» FL .4 ‘ TL»; 90qu «2.41.1 75' WMLK. M guilt. afl— I‘AW lMpJ/M’thobic. 4 mo fiolvudf‘.+l F In Dr. Anfinsen’sflexperiments with RNase A, 8 M urea was to ruin salt bridges in the protein. The urea was then subsequently, removed using an ion exchange Column. m m “mac H—bm*.,m€ at. gamma aw. m cw‘cA W W . I: All of the allosteric effectors of hemoglobin are negative effectors. Of these, H’r is the most im rtant. , *l ‘ -\p° *' in MM», 3% Is +tv. M 02 :‘S a- Posi‘HV‘C h‘izmw 51. +0.1. ($34.55;: W5. 11' Hemoglobin has four different types of histidine residues that participate, directly or indirectly, in the transfer of 02 fiom the lungs to the tissues. H -r\ “‘9 W 3 ‘) grain/trial, 2..) #5411, MA 3) C‘Wm‘M-l WHJL‘M ’1 'Ha' fi'SMlau/rflt's. F A mutation of the N-terminal amino acid residue (i.e. changing the amino acid residue to a different amino acid residue) of the (it-subunits of Hb would seriously afi‘ect the If portion of the Bohr effect. R NAM +64. Miw‘m' H— will 5+?“ [4% M oé~a4~dno WI \ \ \ ' + $3 +01 W P'OL “f M H ; n"# +1»!— flvmt +1 +1 Biological Sciences 102 15. 16. 17. 18. 19. 20. 3of3 Name % E Ten amino acid residues are in a section of a protein. Let’s assume that this section of peptide can form one type of 2° structure, but only one (if there are lefi over residues, we do not necessarily know what they are doing, in terms of structure). The most stable 2° structure this peptide section could be involved in, based on number of H-bonds that are formed, is a reverse 4- mm- ‘g-NM+’M hL- fl’n oL-lru/Qbf gay-m h—Lf = [a IbL-rhVM—J/Al. 74' 5W wu' I $0,,“ cikbwr 5‘41,- ID +H~bmléwwj “fa/v» 00W m m we. W +wo f7me s I . l j The higher altitude in the Rocky Mountains results in a lower p02 , compared to Davis. Let’s assume that this lower p02 results in only 90% loading of the 02 binding sites in hemoglobin when you are vacationing in the Rocky Mountains. Your red blood cells will probably increase their concentration of BPG, in order to deliver more 02 to your tissues. 1‘ [696] W in. m 5%-! “HA-(L a, i-oHc “sewn—4. inuw fin. {@961 inc/ream Han. llkc\;bao-&t;s+1¥lsfi‘camcw 6L 396 Mater/~04, binok in "HA-9. can’i‘ra‘q C‘LVi+‘9. F Crystals of deoxy Mb, kept under a nitrogen atmosphere, display no change when the crystals are exposed to oxygen. However, crystals of deoxy Hb, kept under a nitrogen atmosphere, shatter when exposed to oxygen! The reason for this difi‘erence is that Hb is a much larger protein than Mb. 4’?» . H’b hm A A [5.0 SW ,‘n :H L/p’i'swl M Jr, a, .I M Ma now/5L4. 4» WM Mw. T Carbon monoxide is a lethal allosteric effector for Hb. If we had to label it, we could call it a “ sitive heterotro ic allosteric ffector”. . poT 'kp m1- 0,, ale-Hod m M L-W‘5)+z * urm‘gwt wrat [19 M Hm Wirml'i‘Vi ‘n +(M. lover MM sm_j “j l: Mb is a poorly designed version of Hb. Hi9 Is 24 Bil-9L} +0 W MIG— 0L +13%] \inuj 0'4 4"" 0,, rezzf’vair TLHNL ‘HSSu—La. IFS Mafia“ ‘75 c'wu‘k m W 9"; W0. +3— ‘T' 2° protein structures spontaneously form in the interior of proteins. 20 swudum Alim- gw‘. +1 L. ‘3 Mod g1,ng in alubwqa/r 9M ”\ rM woman“ WM" Wager,” L “Mala; . (Hui-M INK-le RAM-cog. {man “4 WW mm)- ...
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BIS102 Hilt W07 MT2 - lof3 BIS 102 Name_g Winter 2007 Last...

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