A The following plots show an oxygen binding curve for hemoglobin under a certain set ofconditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the bindingoxygen to hemoglobin would be altered by the change in conditions noted.2.a. Increase in pCO2b. Dissociation of native Hb into aß dimers10.80.80.6Y0.40.6Y0.40.20.2pozpO2

The shown in question is Oxygen-Hemoglobin (O2-Hb) dissociation curve where Y axis represent O2-Hb…

Answered: 2. The following plots show an oxygen…

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

See similar textbooks

Similar questions

The Bohr effect related to A. the ability of Hb to bind 02 in the presence of BPG. the ability of myoglobin to expel protons when binding 02. B. the ability of Hb to "take up" protons when binding 02. C. the ability of Hb to release protons when binding O2. D. O E. BPG ionization at 30 torr (the pO2 in veins).
What would happen in terms of pH, T to R state stability, and oxygen-carrying capacity if hemoglobin's Arg141 was replaced with Asp?
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 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM 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 (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 Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION
8. In a patient with anemia, the presence of Heinz bodics in the RBCS was the result of the hemoglobin subunits aggregation due to the oxidation of -SH groups of Hb cysteine residues with active oxygen forms and the formation of disulfide bonds. What metabolic disorders in the RBC can be the cause of this clinical case? To solve the problem: a) indicate which reactions maintain cysteine residues in a reduced state; b) name the coenzyme involved in this process, write a diagram of the process in which the reduced form of this coenzyme is formed; c) indicate the enzyme which deficiency may lcad to a lack of the reduced cocnzyme and be the cause of the clinical case described above.
Q. In hemoglobin protein, an ion pair exists between lysine at position 40 (pka 10) and a beta-chain terminal carboxyl (pka 4). What fraction of these Lys-40/beta-carboxyl are actually in an ion pair at ph 7? а. О b. 0.1 C. 0.5 d. 0.9 е. 1.0
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?
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
. 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.
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…
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.
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…

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS