how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...
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- Glucose reacts slowly with hemoglobin and other proteins to form covalent compounds. Why is glucose reactive? What is the nature of the adduct formed?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 AcidDescribe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?
- What effect on the overall structure of hemoglobin in the presence and absence of oxygen did the substitution of valine for glutamic acid have in the primary structure 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!)A) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?