The cooperative binding behavior of hemoglobin for oxygen is best explained by...

You've discovered a new organism that contains a mutant form of Hemoglobin (red line on right) and are testing its properties in a lab setting at a neutral pH. You've generated the binding data below comparing it to the wildtype (non-mutant; blue line on left) form. Oxygen binding of a new hemoglobin mutant 1.00 - 0.75- Hemoglobin 0.50 - Wildtype Mutant 0.25- 0.00 - 25 50 75 100 pO2 (torr) 1. How does this mutation seem to impact cooperativity? Hint. Look at the slope of the line. [ Select ] 2. Which variant, the mutant or wildtype, has a higher affinity for oxygen? [ Select ] 3. Which variant is a more effective delivery system to the the muscles (~20 torr)? Select ] Fraction of Hb bounw with Oxygen

I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role.   I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only  bind to oxygen, and not release oxygen

Lysozyme cleaves between NAG and NAM residues in bacterial cell walls and is, therefore, classified as a(an) O A. salt bridge, oxidoreductase O B. peptide bond; hydrolase OC. glycosidic linkage; oxidoreductase O D. glycosidic linkage, hydrolase O E. peptide bond; transferase

A mutation of Lysine 82 (in the DPG-binding pocket) to Arginine in beta sub-unit will most likely result in Not enough information Higher than normal binding affinity to oxygen Lower than normal binding affinity to oxygen Normal binding to oxygen

Chemistry Red cells have a volume of ~86 fL. If the concentration of hemoglobin in red cells is ~330 g/L and its Mr is 64,500   b) In the generation of a red cell, the synthesis of all the hemoglobin molecules of the cell takes about 40 h. How many hemoglobin molecules are synthesized in one second per red cell? c) How many subunits (monomers) of hemoglobin are produced in one minute?

. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.

Which of the following did Ruth Benesch and her husband Reinhold Benesch accomplish? Select all that apply. determining the function of 2-3-biphosphoglyceric acid determined the exact location BPG binds hemoglobin by X-ray analysis predicted the location BPG binds to hemoglobin demonstrated that the alpha and beta heterodimers of hemoglobin and conformational changes in the protein were essential to the function of the protein and its cooperative binding