key_mid_2_summer_2006

Key_mid_2_summer_200 - lof2 BIS 102 Name g 23 Summer 2006 Last First K Hilt Second Midterm Score(100 Each question is worth 10 points 1 Amino acid

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Unformatted text preview: lof2 BIS 102 Name g 23 Summer, 2006 Last First K. Hilt Second Midterm Score (100): Each question is worth 10 points. 1. Amino acid analysis of a pentapeptide may: yield five different peaks ' . yield six different peaks +— Cl—‘CJ—JCJD H t c) yield four different peaks d) aandb a + MW." e? aandc a, b, and c ‘ m” E ’2 {a Circle e above correct answer. D t H m r 5' E b 4— NM,“ 9 2. In the Sanger protein sequencing reaction, an N-terminal arginine can be distinguished from an internal ar' ' 6 because: G, the internal arginine will not be yellow ‘hnab b) the N-terminal arginine will be twice as yellow as the internal arginine 311.52. c) the N-terminal arginine will extract into the upper ether phase Lalo—c. d) a and b e) a and c t) b and c Circle the above correct answer. 3. A mutation of the C-terminal histidine in the B-subunits of hemoglobin to an arginine would result in: a reduced H)r portion of the Bohr effect, but no change in the C02 portion of the Bohr effect an increased H)r portion of the Bohr effect, but no change in the C02 portion of the Bohr effect c) an increase in both the H+ portion and C02 portion of the Bohr effect d) a decrease in both the H+ portion and C02 portion of the Bohr effect e) no real change in either the IV or C02 portion of the Bohr effect. Circle the above correct answer. 4. It is possible to obtain pure crystals of deoxy Mb in a N2(g) atmosphere. It is also possible to obtain pure crystals of deoxy Hb in a N2(g) atmosphere. When these crystals are exposed to 02(g), one set of crystals shatters! Is it the Mb or Hb crystals? Explain why they shatter. Give a detailed explanation. The molecular weights of Mb and Hb are 17,000 and 68,000, respectively. *3 me. BinaA/lflfi 01 (€4.41; in e. large eke-my it. 3‘ “at we on W‘ shrutLA'V-v‘e , + 7 5. A tyrosine side chain in a protein has its pKa increase. This could be due to: a) a histidine residue moving into close proximity $a»\$<. ¢ ” b) a glutamate residue moving into close proximity hm, {mixers 0 Wat-3" 0'” Y c) a lysine residue that was close, moving further away +r M, «ii-wows 0 WW Wu H’ d) the tyrosine residue moving from the interior of the protein to the surface of the protein 4445‘ e aandb \ andc c‘J’i’. g) aandc Y Pan 2 Q Circle the above correct answer. 0 0‘ £30,00va 20f2 BIS 102 Name a) 6. The number of moles of 02 that will be released if a liter of blood containing 40 g of hemoglobin is transferred from 60 torr, pH 7.6 to 15 torr, pH 7.2 is approximately: W " 5.???“ a: 1.99x 10'3 mo] 02 “53”” 3"va H 4.99x10“mo102 H, X H J: c) 3.52x10‘4mo102C5-Wz “0 wilt“: d) 1.36x104m0102 235’" 50“" Me 0; e) 5.02x10'2m0102 -3 , _ f) noneoftheabove (2'3g‘l’ '“Q<0'35) 7. Amino acid analysis of one mole of a peptide yields two moles of phenylalanine, one mole of cysteine, one mole of lysine, one mole of glycine, and one mole of methionine. Determine the sequence of this peptide from the following information: a) treatment of the intact peptide with chymotrypsin yields free phenylalanine, free glycine, and a tetrapeptide containing lysine, phenylalanine, cysteine, and methionine; b) treatment of the original peptide with cyanogen bromide yields two tripeptides, one containing glycine and phenylalanine, and the other containing lysine, methionine, and cysteine; c) treatment of the original peptide with trypsin yields a dipeptide containing lysine and cysteine, and a tetrapeptide containing glycine, methionine, and phenylalanine; (1) treatment of the original peptide with carboxypeptidase A and B yields glycine. Give the sequence, using the one-letter amino acid code, in the space that follows: g; - is ' M -' F -.- F ‘- Q r z gar e M r c. 53 M 8. A student has identified the following short amino acid sequence from eir purified protein: A-V-E-P-G-R-W—K-F A, 3 a) What type of secondary structures are possible in a protein? , Orv-halt"; 65»-pl€atieo 5W' rWSc WV“ b) Which protein secondary structure(s) do you think the above peptide sequence could participate in? Explain. +| “ "' (merge. Mn, m (a W pug-ad” a. ‘Wffik a... +1 “n.9, kwfl no M: vat, ‘l’un : 9 he». \LiniLl E, is swmu. E] E fi M’ 9. Imagine that the p02 in Davis is 100 torr. You go on vacation to the Rocky Mountains where, at 10,000 it. altitude, the p02 is only 80 torr. Do you think that your red blood cells will make a higher or lower concentration of BPG to adapt to this higher altitude? Explain. Why is this change in [BPG] effective? {*1 . a Hizaku [8961, MM BPG, run-m m L «ewr‘l‘nw 5% a1 «la; 0; +3 In; mus-wt, We +0 HM» rt . 11054 :5 W. 3P9 nm 14% + a akin 6". up“, «‘4 W Cat-vi . M W W! O 1 014, +0 5, . +2. 10. Imagine that a strange new form of hemoglobin has n 'scovered. It has the same a- and B-subunits that normal Hb has, but instead of being 0:202 it is 0t3l33. How many salt bridges do you think this new form of Hb has? Explain. Include a simple calculation as part of your answer. Q MW“ M *3 .. W w*“'\\ ‘P 2- P“;ij [33.64% a Y 5*” Fizz: a: 19.; fit) LI W e, W l' " ...
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This note was uploaded on 06/07/2008 for the course BIS 102 taught by Professor Hilt during the Winter '08 term at UC Davis.

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Key_mid_2_summer_200 - lof2 BIS 102 Name g 23 Summer 2006 Last First K Hilt Second Midterm Score(100 Each question is worth 10 points 1 Amino acid

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