BIS102 Final F95 Key Scholey

BIS102 Final F95 Key Scholey - NAME FIRST Student...

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NAME: FIRST Student Identification Number: BIOLOGICAL SCIENCES 102-01, Fall December Final Exa There are 11 pages in this exam including the cover sheet and 1 sheet of graph paper. Please count before you start to make sure all are present. Write your name on each page of the exam. Write your answers in the space provided below each question. If you need more space use the back of page and that you have continued your answer on the back. Do not use additional paper. For calculation problems a line of calculations leading to your answer must be shown to obtain full credit, Whenever appropriate, include the (e.g., mmol, etc.) in your answer. 2.1 3.9 9.1 2.2 9.2 1.8 6.0 10.8 9.1 2.2 10.0 9.0 2.2 125 20 25 5 20 50 Note: Academic Senate regulations prohibit reassessment of exams (or any other coursework) once grades have been determined. In other words, final exams cannot be regraded. Be sure that your work and reasoning are clearly presented and your answers are clearly indicated, otherwise your work may be graded more harshly you feel is warranted and you will have no opportunity for re-evaluation.
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NAME: LAST 1. (20 points) FIRST 2 (a) (5 points) Draw the reaction that produces the covalent bond which links ammo acids into proteins, and this bond. In other words, draw the structures of the reactants and the products of the reaction, and then name the bond formed by the reaction. (5 points) The free energy for the formation of a protein from the individual ammo acids is positive. In thermodynamic terms, how do cells accomplish this process? (c) (10 points) Name and briefly (or describe) the four types of noncovalent interactions that drive the formation of the tertiary and of proteins.
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NAME: LAST 2. (25 points) 3 (a) (5 points) For each of the pairs below, circle the conjugate base. RCOOH (20 points) A biochemist mixes 100 of 0.5 of acetic acid with 400 of 0.5 M What is the (The of acetic acid is 4.7). 3. (20 points) A 0.1 M solution of glucose-l-phosphate is incubated with the enzyme of to ‘At equilibrium, the concenuation of is 9.6 x 10 M and that of glucose-l-phosphate is 4.5 x M. Calculate the constant (Keq’) and standard free energy change for reaction (R = 8.315 T 298K).
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