A) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain.
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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?
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- How does the difference between the -chain and the -chain of hemoglobin explain the differences inoxygen binding between Hb A and Hb F?What are the two critical amino acids near the heme group in both myoglobin and hemoglobin?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?
- Hemoglobin is composed of how many polypeptide chains thatchange during development?What are two features D-Glucosaminate-6-phosphate Ammonia-lyase structure that make either it different OR similar to haemoglobin?The T-state of hemoglobin is favored over the R-state in blood under which of the listed conditions?
- how do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...Which structure represents d-erythrose?The molecular formula for glucose is C6H12O6. What would be the molecular formula for a polymer made by linking ten glucose molecules together by dehydration reactions? Group of answer choices A. C60H120O60 B. C60H102O51 C. C60H100O50 D. C60H111O51 Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)In sickle-cell disease, as a result of a single amino acid change, the mutant hemoglobin tetramers associate with each other and assemble into large fibers.…