The proximal histidine in hemoglobin is where CO2 binds hemoglobin in order to be transported through...
- The proximal histidine in hemoglobin
- is where CO2 binds hemoglobin in order to be transported through the circulation as carbamate.
- is where H+ binds to the hemoglobin to cause the Bohr effect.
- forms a hydrogen bond with oxygen when oxygen binds hemoglobin.
- anchors the heme to the globin.
- makes the binding of 2,3-BPG to hemoglobin possible.
Homework Answers
e. makes the binding of 2,3-BPG to hemoglobin possible.
In myoglobin protein, a site is occupied by the residue of histidine called as proximal histidine. This makes the binding of 2,3- bi phosphoglycerate which lowers the oxygen affinity towards the hemoglobin, which releases oxygen easily.
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The proximal histidine in hemoglobin
is where CO2 binds hemoglobin in order to be
transported through...
ter 9. Hemoglobin and Myoglobin Which of these is not found in myoglobin? A) alpha helix...
ter 9. Hemoglobin and Myoglobin Which of these is not found in myoglobin? A) alpha helix b) beta sheetc) heme group, d) globular folding pattern • Which statement about hemoglobin is not true? A) it is globular b) it contains helix loop-helix c) it has three subunits d) it has heme groups · The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these - The...
vols " statement about hemoglobin is not true? A) it is globular b) it contains helix-...
vols " statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin from its T-form to its R-form results in: a) Loss of BPG b) Does not result in release of CO2 c) cooperative...
Chapter 9. Hemoglobin and Myoglobin 1. Which of these is not found in myoglobin? A) alpha...
Chapter 9. Hemoglobin and Myoglobin 1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these...
How does BPG, or 2,3-biphophoglycerate produce the shift in the oxygen bunding curves shown? (BPG works to effect the binding of oxygen to hemoglobin) Circle the correct choice. a) BPG binds to the R...
How does BPG, or 2,3-biphophoglycerate produce the shift in
the oxygen bunding curves shown? (BPG works to effect the binding
of oxygen to hemoglobin) Circle the correct choice.
a) BPG binds to the R state of hemoglobin tetramer.
b) BPG binds to the T state of hemoglobin tetramer.
c) BPG binds to the heme group, which blocks access to the
oxygen
d) BPG oxidizes the iron (II) in the heme group to the iron
(III), preventing oxygen from binding.
1.0...
Which of the following statement(s) is/are TRUE regarding the binding of oxygen to hemoglobin? A. The pH difference bet...
Which of the following statement(s) is/are TRUE regarding the binding of oxygen to hemoglobin? A. The pH difference between the lungs and the surrounding tissues that decreases efficiency in oxygen transport is known as the Bohr effect. B. 100% of CO2 is transported by formation of a carbamate bond with the amino terminal residues in the hemoglobin chains. C. 2,3-Bisphosphoglycerate stabilizes the T state. D. All of the statements are true.
Regarding the effects of the affinity of hemoglobin when 2,3-biphosphoglycerate (BPG) is regulating, analyze the biochemical...
Regarding the effects of the affinity of hemoglobin when 2,3-biphosphoglycerate (BPG) is regulating, analyze the biochemical mechanisms that occur to cause the catch and release of oxygen in this manner. Which of the following structural changes occur when deoxyhemoglobin binds to oxygen? Choose the two correct answers and briefly explain why the other two are incorrect: 1.) The proximal histidine (His F8) moves helix F towards the planar heme. 2.) The heme releases CO2 from the other subunits. 3.) A...
1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c)...
1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme...
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group 1. d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
4. Noncompetitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c)...
4. Noncompetitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis. 5. Which statement best describes the effect of pH upon enzyme catalyzed reactions? a) rate increases with increasing pH b) rate decreases with increasing pH c) rate increases with increasing pH until the denaturation pH is reached d) every enzyme has an optimum pH...
biochemistry if you could please help me answer the following questions! EFT i 11) (6 pts)...
biochemistry
if you could please help me answer the following questions!
EFT i 11) (6 pts) Which types of symmetry are possible for a protein with six (6) identical subunits? (Select all correct answers) a) cyclic C b) cyclic C3 c) dihedral D2 d) dihedral D e) octahedral o f) icosahedral ро, Yo₂ - pO₂+ Pso 12) (6 pts) What is the fractional saturation of oxygen binding to myoglobin when the partial pressure of oxygen is 1.5 torr and dissociation...
ter 9. Hemoglobin and Myoglobin Which of these is not found in myoglobin? A) alpha helix b) beta sheetc) heme group, d) globular folding pattern • Which statement about hemoglobin is not true? A) it is globular b) it contains helix loop-helix c) it has three subunits d) it has heme groups · The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these - The...
vols " statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin from its T-form to its R-form results in: a) Loss of BPG b) Does not result in release of CO2 c) cooperative...
Chapter 9. Hemoglobin and Myoglobin 1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these...
How does BPG, or 2,3-biphophoglycerate produce the shift in
the oxygen bunding curves shown? (BPG works to effect the binding
of oxygen to hemoglobin) Circle the correct choice.
a) BPG binds to the R state of hemoglobin tetramer.
b) BPG binds to the T state of hemoglobin tetramer.
c) BPG binds to the heme group, which blocks access to the
oxygen
d) BPG oxidizes the iron (II) in the heme group to the iron
(III), preventing oxygen from binding.
1.0...
1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group 1. d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these 4. The transition of hemoglobin...
4. Noncompetitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis. 5. Which statement best describes the effect of pH upon enzyme catalyzed reactions? a) rate increases with increasing pH b) rate decreases with increasing pH c) rate increases with increasing pH until the denaturation pH is reached d) every enzyme has an optimum pH...
biochemistry
if you could please help me answer the following questions!
EFT i 11) (6 pts) Which types of symmetry are possible for a protein with six (6) identical subunits? (Select all correct answers) a) cyclic C b) cyclic C3 c) dihedral D2 d) dihedral D e) octahedral o f) icosahedral ро, Yo₂ - pO₂+ Pso 12) (6 pts) What is the fractional saturation of oxygen binding to myoglobin when the partial pressure of oxygen is 1.5 torr and dissociation...
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