Which of the following is not a feature of the Bohr effect? Group of answer choices A. a histidine protonates at an elevated pH value than free imidazole B. ion-pair formation increases proton affinity to hemoglobin C. noncovalent carbon dioxide binding assists oxygen unloading in tissues D. new salt bridges are formed from the covalent attachment of carbon dioxide E. the covalent attachment of carbon dioxide to hemoglobin causes a pH drop

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?

Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2

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 dimers

5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 Symbols: a Dсм 23 Torr • DCM 50 Torr x DCM I00 Torr o, 0 Torr DCM; О, 23 Torr DСМ Д, 50 Torr DСМ x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Kd for O2 binding is defined for 0 and 100 Torr of dichloromethane Kd Hb(O2)n nO2 Hb + Be sure to label the axes, indicate the units on both axes, and make the Hill plot so that the values of Kd are equivalent to those on the saturation plot above. Indicate whether cooperativity, as indicated by the Hill…

1. Hemoglobin researchers have discovered more than 500 naturally occurring hemoglobin mutations. The majority of these results from single amino acid changes. Some of these mutations result in clinical illness or symptoms, but many show no outward effects. Some examples are:    HbS (sickle cell Hb)-substitutes Val for Glu on the surface  Hb Cowtown - eliminates an ion pair used in T-state stabilization Hb Memphis - surface uncharged polar aa for another of similar size on the surface  Hb Bibba-substitutes a Pro for a Leu in an α-helix Hb Milwaukee - substitutes a Glu for a Val  Hb Providence- substitutes a Asn for a Lys that normally projects into the central cavity   Hb Philly - substitutes a Phe for a Tyr, disrupting hydrogen bonding at the aß interface.   EXPLAIN your choices for each of the following:   a) The Hb variant least likely to cause pathological symptoms    b) The variant(s) most likely to show pl values different from that of HbA   c) The variant(s) most likely to show…

There is an animal that uses almost 100 percent of the oxygen in its blood. Analyzing the Hb of this animal, it’s found that 2,3-BPG does not bind to Hb, but bicarbonate ions do. Knowing that bicarbonate ions are strong negative allosteric effectors, what do you make of these findings? Why is the animal’s Hb not responsive to 2,3 BGP, but responsive to bicarbonate ions?

Will a mutation from Distal histidine to phenylalanine shift the binding curve of hemoglobin?Will it shift the curve to the left or right, shift to myoglobin or no longer bind to O2?