Which of the following are roles of the distal histidine in hemoglobin? to help to keep the heme in the pocket through a coordinate covalent bond. to help to keep myoglobin in the ferric (Fell) state. to reduce the affinity of CO for the heme iron. to help to protect the heme from H-bonding with water. to help to protect the heme from irreversible oxidation
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- Allosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformationThe primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.The amino acid in Hemoglobin that is most found to be most sensitive to pH changes, and hence affects Oxygen binding process around pH 7 is Valine Tyrosine Histidine Aspartic Acid
- A researcher, in a study involving acid-base properties of RBC's notices the resistance of change in pH, when a small amount of acid or base is added to it. Buffering action of hemoglobin in RBCS is most likely attributed to presence of which of the following factors in the globin chains? Alpha helical structures В Beta pleated sheets C Ferric state of iron D Ferrous state of iron E Histidine residuesOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).Cows that graze on spoiled sweet clover, which contains dicoumarol, die from hemorrhagic disease. The cause of death is defective prothrombin. However, the amino acid composition of the defective prothrombin is identical to that of normal prothrombin. What is the mechanism of action of dicoumarol? Why are the amino acid compositions of the defective and normal prothrombin the same?
- Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environmentsWhich of the following proteins serves a structural function (not an enzymatic function)? chymotrypsin thrombin elastase collagen trypsinWhich of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.
- Hemoglobin glycation (so named to distinguish it from glycosylation, which is the enzymatic transfer of glucose to a protein) is a non-enzymatic process that involves reaction of the N-terminal amino group of hemoglobin and glucose. The amount of glycated hemoglobin (GHB) is usually about 5% of total hemoglobin (and corresponds to a blood glucose concentration of 120 mg/100 mL). However, in people with untreated diabetes this value may be as high as 13%, which indicates an average blood level of about 300 mg/100 mL -dangerously high. One of the aims of insulin therapy is to maintain GHB values of about 7%. Draw a possible chemical scheme for the glycation of hemoglobin.One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)Amino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.
