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UM BCH 380 - Practice Test

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BCH 380; Spring 2012 Name:______________________________1. Draw the amino acid with the one letter code E in its different ionized forms goingfrom pH of 0-14 and calculate the pI given the following pKa’s:[ acid group= 2.2, amino group= 9.3, R group = 4.2].2. Draw D-serine using a Fischer projection and R-Serine using a Newman Projection.3. Draw the dipeptide YF and show the position of the Phi and Psi angles.1BCH 380; Spring 2012 Name:______________________________4a) From the following graph, state the type of inhibition for Panels B, C, and D and describe how Vmax and Km change for each.4b) In Panel A (no inhibitor) if the equation for the line was (y = 2x + 5), calculate Km, Vmax and kcat for this enzyme with a concentration of 1 x 10-6 M.5) Which of the following are considered as noncovalent bonds?A) electrostatic interactions B) hydrogen bonds. C) van der Waals interactions. 2BCH 380; Spring 2012 Name:______________________________D) All of the aboveE) None of the above. 6) Which of the following amino acid residues would most likely be buried in the interior of a water soluble, globular protein? A) Asp D) Lys B) Ser E) GlnC) Phe 7) Why is the peptide bond planar? A) Bulky side chains prevent free rotation around the bond. B) It contains partial double-bond character, preventing rotation. C) Hydrogen bonding between the NH and C=O groups limits movement. D) None of the above. E) All of the above. 8) The ________________________ β-sheet structure occurs when the two strands are oriented in opposite directions (N → C).9) Which secondary structure is stabilized by CO and NH hydrogen bonding within the peptide chain _________________.3BCH 380; Spring 2012 Name:______________________________10) The difference between the standard-state free energy, ΔGº, and the biochemical standard-state free energy is that ΔGº’ refers to the standard free-energy change at ________.11) Allosteric enzymes can be identified because the plot of initial velocity, V0, versus substrate concentration, S, is not hyperbolic but __________________ -shaped.12) A __________________ inhibitor has a structure similar to the substrate and reversibly binds to the active site of the enzyme.13) Allosteric proteins A) contain distinct regulatory sites and have multiple functional sites. B) display cooperativity. C) always consist of several identical subunits. D) a and bE) a, b, and c 14) The model describing allosteric regulation that requires all subunits to be in the same state is called the ________.A) concerted modelB) syncopated modelC) cooperative modelD) equilibrium model4BCH 380; Spring 2012 Name:______________________________E) None of the above 15) Allosteric modifiers alter the equilibria betweenA) the ES stateB) the R and T forms of a proteinC) the forward and reverse reaction rate D) the formation of product and it’s reverse reactionE) All of the above16) From the above drawing, state what type of inhibition each is showing and draw the appropriate E, S, I reaction equilibrium.5BCH 380; Spring 2012 Name:______________________________17a) What is the pH of a 0.3 M solution of an acid given the Ka is 1.75 x 10-5.17b) What is the resulting pH after addition of 0.5 mole equivalents of base i.e. [0.15 M NaOH].Appendix/Formulae1/Vo = (Km/Vmax) x (1/[S]) + 1/Vmax6BCH 380; Spring 2012 Name:______________________________Vmax =


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UM BCH 380 - Practice Test

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