11. Which of the following best describes what happens when hemoglobin bindsbisphosphoglyceric acid (BPG)?A. Binding of BPG leads to tighter binding of oxygen.B. Binding of BPG allows maternal (adult) Hb to bind oxygen more tightly than fetal Hb.C. Binding of BPG is important to the allosteric nature of hemoglobinD. Binding of BPG causes the subunits of hemoglobin to separate.

Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…

Answered: 11. Which of the following best…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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3. а) The haemoglobin molecule is designed to transport oxygen around the body. With reference to the different levels of organization of polypeptides explain how this molecule achieves its function. • Both starch and cellulose are polymers made up of glucose molecules. They are found in plants but serve different functions in the plant. In no more than 200 words: identify the function of starch and cellulose in plants. explain how glucose is able to form these compounds. relate the structures you have described above to their function(s).
1. All oxygen inhaled by animals and transported around their bodies is destined for specific locations in the body. Once oxygen reaches protein complex IV of the electron transport chain (ETC) it begins its vital task of pulling electrons away from protein complex IV. In short, a set of chain reactions are triggered at protein complex IV. From here 2 electrons are taken from complex III, which then takes two electrons from complex II, or l. a) Use a diagram and your own words to describe how a proton-motive force created by the ETC generates ATP. Make sure you label your diagram correctly and include; inner mitochondrial membrane, hydrogen ions, ADP, P, intermembrane space, ATP synthase, mitochondrial matrix, and ATP.
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43. What would happen if red blood cells had mitochondria?
Why is the decreased affinity of fetal hemoglobin for BPG advantageous? With fewer BPG molecules bound to heme, there are more heme residues available for O2 binding. O A. B. Decreased BPG binding biases the fetal hemoglobin toward the R state. C. More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state. BPG is more available to bind to fetal myoglobin. helping to release O2 in fetal muscle tissue. D. 47
Which of the following statements is true? Select any/all answers that apply. O A. Both Mb and Hb bind 02 cooperatively. O B. Mb and Hb have similar affinities for BPG (2,3-bisphosphoglycerate). O C. Both Mb and Hb transport oxygen within the blood. O D. A single Mb molecule and a single Hb subunit have similar tertiary structures. O E. Both Mb and Hb contain multiple oxygen-binding sites.
. 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.
4. PFK-1 is tightly regulated with multiple potent allosteric regulators. Name three of these regulators and explain how they influence the activity of PFK-1.
19. You want to compare the amount of HIF-1 alpha in cells in hypoxic conditions and normal conditions. A. Describe in step-by-step format 2 approaches you could take. Include in controls you would need. B. For the 2 approaches you could take, indicate which one you would rather do and why.
The hemoglobin in mammalian blood is usually thought of simply as increasing the amount of O2 that can be carried by each litter of blood. Explain how the presence of hemoglobin in the blood also makes possible the rapid uptake of O2 by the blood as it flows through the lungs.
Which of the following is the metabolic conversion of bilirubin in the small intestine a. Macrophages b. Urobilinogen c. Hemoglobin d. Neutrophils
a quinine tablet is taken to prevent malaria, t days later, 50(0.23)^t mg remain in the body. A. How much quinine is in the tablet? At what rate is it decaying? B. How much quinine remains 12 hours after tablet is taken?

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