BIS102 Hilt Summer06 FINAL

BIS102 Hilt Summer06 FINAL - lof2 Biological Sciences 102...

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Unformatted text preview: lof2 Biological Sciences 102 Name Summer, 2006 Last, First K. Hilt Final Exam Score (200): PH = PKa + 10% {[basel/[acidl} AG = AH - TAS F = ((11 <12)/(8 r2) Vo = {Vmax [3]} / {Km + [3]} PKa’s of the side chain R—groups are: D (3.9), E (4.2), H (6.0), C (8.3), Y (10.1), K (10.5), and R (12.5). PKa’s of amino acid a-amino group (9.60) and a-carboxyl group (2.10). PKa’s of N-terminal oligopeptide a-amino group (7.40) and C-terminal a-carboxyl group (3.6). 1. (25 pts.) Fill in the ten missing values in the following enzyme purification table: M) Volume [Protein] Imagine that twenty-five I.U.’s of enzyme Z were catalyzing the above reaction, from lefi to right, for one minute under Vmx conditions in a 3.00 ml assay volume. The assay is buffered with 25 mM phosphate buffer, pH 7.00. The pKa’s of phosphate are 2.12, 7.21, and 12.32. The pH at the end of one minute will be: '7 . 1a \ t 0 «l . Use the back of this paper for calculations. There is no partial credit. However, you must show your work to receive credit. 3. (10 pts.) Draw the structure of phosphatidylserine in the form that would predominate at pH 7. This phospholipid must contain oleic acid at position #1 and a-linolenic acid at position #2. 4 z ‘3 o _ + 2- ‘? MWC u, ‘5 1311 l 4. (20 pts.) The &.is leak histidine in Hb provides a H-bond to oxygen at a heme. The acid ' portion of the Bohr effect involves a histidine located at the Q. ~ +or m‘ mm. of the —s wbum +5 The pro fimafl histidine provides a critical link between the heme and the protein subunit that it is part of. (Fill in each blank with one or more words). eaok blank *5- 20f2 BIS 102 Name @ 5. (20 pts.) A(an) a «i— fiiwih] 00’ column consists of a polar matrix bead, an at mi? 3 , and a biologically specific ligand, all cova ently attached to each other. The column may be eluted by changing is} T 3, increasing the SaM " 3 concentration, or pouring through the ligand. To determine the effectiveness of the column, each test tube of solution collected from the column is assayed for protein concentration using the Era} QML + 3protein assay. In addition, each fraction is also assayed for mm afa‘iiztivity. Mathematically, these two assays are expressed together in a purification table as “specific activity”. In addition, we might assess purity by running several types of analytical gels. One such gel employs a * 3 pH gradient established using am. la ol 4—“. and a power supply. (Fill in each blank with one or more wordsi. 6. A peptide has the following sequence: E-D-M-K-C-Y. Answer each of the following questions: “(3 pts.) a) Treatment of the above peptide with asp—N would give the following fi'agment(s): fl 0,“ 0’ b + brutch (10 pts.) b) Draw the expected elution profile for the fourth cycle of the above peptide using the Edman chemistry in the protein sequenator. Use the axes given below. Label each axis and peak(s). Numbers on the x- axis have been provided. Sketch in your peak(s) carefully. *\ 1“: 'V‘ 3. PT“ " K AA [—— O\UWH M Jr €- 0 TWIN. +t 50 (20 pts.) c) The net charge of the intact peptide at pH 8.2, to the nearest 0.01, is - 2 . '4 7— You may use the back of this page for calculations. There is no partial credit. However, you must show your work to receive credit. 7. (35 pts.) Weak bonds are very important in biochemistry. Of the four weak bonds, the one that is most important in determining native 3° and 4° structure is M My? kebt‘c. 69W . In contrast, the weakest of the four weak bonds is \l m éLM DJO-ALL . However, even it plays critical roles in the close confines of the who. vi w of proteins and in Membra. vx 0— s (not a protein). The weak bond that is critical in lowering the energy of proteins, by allowing peptide bonds to exist in n W 0 KM protein interior, is l—l -— banal/2.. . . One of the weak bonds, / namely { mm in WAA. , has its force of attraction related to l/ri. (Fill in each blank with one or morawords). W Hawk l' 5" kt.)th M w. 8. (20 pts.) The number of moles of NaOH required to raise the pH of 350 ml of 0.200 M arginine buffer, pH 2.60 to a final pH of 12.40 is: O . l \ "I moles. You may use the back of this paper for calculations. There is no partial credit. However, you must show your work to receive credit. 9. (15 pts.) The movement of H00 3" and C l — through the anion exchange protein in the plasma membrane of red blood cells, helps get rid of excess C 0;. present in the tissues of animals. An enzyme, carbonic anhydrase, assists this process by converting L. O 7. to H CO 3"" ; the latter a more water soluble form of the former. (Fill in each of the blanks with a word or chemical structure). e444. blmk +3 {tug . , Cm) ny—E-D—M—Krc-w - won-l " i L. 3“! g :C~ 2 12.. r (043,9) ,4: (19:13), 11.6- a, L2) ‘1 52:9?” “9’8, (0.350£)(o.2mr4 ecu-3): 0,07% we Mj 2.00: 210+»! 1" \ 0'3“ 3: 0.5‘0 F‘— I A 3.”! '-‘— “x 6.: qu: 0-3” 1.25?‘ A -'r @,2u)(o. 07o woe «r33 = lo =- QALIXO. 070 Me :: fro-5‘1 “03L m4“ 2 o. 01;? + CLO-,0 + o.030 0.111.? m4 4‘5 o.l|‘7 mi ...
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This note was uploaded on 10/07/2009 for the course BIS 52192 taught by Professor Enochbaldwin during the Summer '09 term at UC Davis.

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BIS102 Hilt Summer06 FINAL - lof2 Biological Sciences 102...

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