Practice_Exam_II_ans - Spring 2004 BCHS 3304 Exam II...

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Spring 2004 BCHS 3304 Exam II Review- 1). A sequence of residues in a certain protein is –S-G-P-G-. The sequence is most probably part of a(n): a). β -turn b). Parallel β -sheet c). α -helix d). Collagen fiber e). Antiparallel β -sheet. (a), β -turn. 2). Which equation describes the binding isotherm (curve) of Hb for O 2 ? a). Hb(O 2 ) n+1 + H +  Hb(O 2 ) n + O 2 . b). Mb(O 2 ) + Hb  Mb + Hb(O 2 ). c). p50 1/affinity d). K = [Hb] [O 2 ] [Hb(O 2 )] e). YO 2 = ____(pO 2 ) n ___ (p50) n + (pO 2 ) n : (e), this equation describes the fractional saturation phenomena for the binding of O 2 to hemoglobin. 3). The salting out procedure is a process where salts (ions) are added to a protein solution such that the high ion concentration competes with proteins for favorable interactions (solvation) with water, resulting in the precipitation of the protein. Would you expect the salting out phenomenon to be most effective when the pH of the protein solution was above, below, or at the isoelectric point of the protein of interest? a). pH above the pI b). pH below the pI c). pH = pI d). pH does not matter (c), the salting out procedure will be most effective when the pH of the solution is = isoelectric point of the protein of interest as a protein is usually least soluble when its net charge = 0.
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4). An enzyme catalyzes a reaction without itself being __________ in the process. It does this by __________ of the reaction. Enzymes preferentially bind the ____________ in an ideal situation. The extent to which an enzyme will catalyze a reaction is ultimately dictated by the ___________ for the reaction. : An enzyme catalyzes a reaction without itself being consumed/altered in the process. It does this by lowering the activation energy of the reaction. Enzymes preferentially bind the transition state in an ideal situation. The extent to which an enzyme will catalyze a reaction is ultimately dictated by the equilibrium constant for the reaction. 5). At what concentration of denaturant (guanidinium hydrochloride) will a particular protein unfold if the value of G H2O D-N = 34.0 kJ mol -1 and the m D-N = 10.5 kJ mol -1 M -1 ? a). 32.4 M b). 3.24 M c). 0.324 M d). 0.31 M e). 3.1 M (b), G D-N = G H2O D-N - m D-N [denaturant]; setting G D-N = 0, [denaturant] = G H2O D-N = 3.24 M m D-N 6). Which of the following most accurately describes the driving/stabilizing force for the α -keratin 4 ° structure? a). Cys disulfide bonds hold the α -keratin α -helices together. b). Hydrogen bonds hold the α -keratin α -helices together. c). Lysine semi-aldehyde bonds hold the α -keratin α -helices together. d). The amphipathic nature of the α -keratin α -helices favors the association of the helices into a coiled coil structure. e). All of the above.
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Practice_Exam_II_ans - Spring 2004 BCHS 3304 Exam II...

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