A point mutation in Hb diminishes hydrophobicity at the heme. Which of the following impacts would you predict? . Increased oxidation of Fe2+ and loss of O2 binding b. Decreased negative charges needed at the dimer/dimer interface to stabilize the T-state c. Decreased positive charges needed at the dimer/dimer interface to stabilize the T-state d. Shift the O2 binding curve of Hb to the left e. Decreased affinity for BPG in the T-state
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A point mutation in Hb diminishes hydrophobicity at the heme. Which of the following impacts would you predict?
| . |
Increased oxidation of Fe2+ and loss of O2 binding |
|
| b. |
Decreased negative charges needed at the dimer/dimer interface to stabilize the T-state |
|
| c. |
Decreased positive charges needed at the dimer/dimer interface to stabilize the T-state |
|
| d. |
Shift the O2 binding curve of Hb to the left |
|
| e. |
Decreased affinity for BPG in the T-state |
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- If there was a molecule that causes Hb to be more stable in the T state, this molecule would: a. Generally, raise the affinity of Hb for O2 b. Generally, lower the affinity of Hb for O2 c. Generally, cause Mb to favor the R state while Hb is in the T state d. Generally, cause Hb to dissociate into αβ dimersThe first step of the lysozyme reaction (catalytic mechanism) is shown in the figure below. Which statement regarding lysozyme is true? Glu 35 HO O(NAM) R (NAG) Asp 52 a. The local environment of Asp 52 significantly changes its pka. b. Glu 35 has an unusually low pKa due to its hydrophobic environment. c. Glu 35 provides acid/base assistance during catalysis. d. Glu 35 acts as a nucleophile during catalysis.Which of the following best explains why fetal hemoglobin (HbF) has higher affinity for oxygen than HbA? a. HbF binds 2,3-bisphosphoglycerate with lower affinity b. One of the coordination positions of HbF is occupied by an Asp residue c. Oxygen binding is not cooperative in HbF d. The Fe-O bond is shorter in HbF e. The hemes of HbF and HbA have different structures
- The steps of the chymotrypsin mechanisms are listed below (1-7). Put the steps of chymotrypsin mechanism in the correct order. Figure representing chymotrypsin mechanism is given for reference. a.The portion (N-terminal end) of original substrate with the new C terminus diffuses away b. Substrate binding c. His 57 catalyzes removal of H from Ser 195 hydroxyl; Ser 195’s nucleophilic O attacks carbonyl C of substrate; tetrahedral intermediate is formed d. Water binding; water is deprotonated by His 57; resulting OH nucleophilically attacks carbonyl of remaining substrate; tetrahedral intermediate is formed e. His 57 donates H to N of…Which of the statements below regarding glyphosate are true? (Choose all true statements) A.Glyphosate interacts with EPSP synthase because it resembles the substrate S-3P B.The interaction of S-3P is necessary for glyphosate binding. C.Glyphosate likely binds to both conformations of EPSP synthase shown in question 7. D.Glyphosate decreases Km for S-3P and thus likely the increases the affinity of the enzyme for substrate E.Glyphosate likely increases feedback inhibition by the product of the reaction EPSPHb Waterloo has an AspG1 (94)a to Gln mutation. Which of the following statements is TRUE? It has a high affinity for O2 because a hydrogen bond in the T state is broken. It has a low affinity for O2 because a hydrogen bond in the R state is broken. The Bohr effect is diminished due to the loss of the primary binding site of the Bohr proton. The mutant has a lower affinity for O2 due to the loss of a hydrogen bond present in the T state. Cooperativity in the mutant is increased because the mutation occurs in the switch region.
- In one type of hemoglobin mutant the amino acid change generates a strong ionic interaction stabilizing the T state conformation, but only under conditions of lower pH, e.g., at pH 7.2 compared to pH 7.6. Explain what effect this mutation would have on the amount of O2 delivered to the tissue. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the R state in tissues.Given: Factor VIIa is a man-made protein analog to Factor VII, which is involved in coagulation. (Answer a, b, and c)a. Identify both a competitive and non-competitive inhibitor for Factor VIIa b. Draw a graph showing how both of these molecules will change the Velocity/[S] graph, and explain why this is the case. c. What would a graph look like if both inhibitors were added?We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
- In addition to O, binding, changes in other chemical conditions can result in hemoglobin changes. pH is one of those factors. It can be understood by reaction #1. Red blood cells have the enzyme Carbonic Anhydrase which catalyzes reaction #2. Using the two reactions explain how pH contributes to the transfer of O2 from the lungs to the tissues. H-Hb* + O2 Hb-O2 + H* Reaction #1 CO2(aq) + H2O= H* + HCO3 Reaction #2We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.