e1.00.5-06.Answer the questions below about hemoglobin and myoglobin.a. Sketch and label the binding curves of Mb, Hb, and Hb below.pº₂b. In the scenarios below for Hb, indicate what effect they would have on thebinding curve and give a brief explanation?ScenarioDecrease in theconcentration ofcarbon dioxide(CO₂)Distal histidine(the histidine thataids in molecularoxygen binding)mutation tophenylalanineHigh heat andextreme pHchangesPredict if the normal bindingcurve of Hb will shift right(Hbt), left (HbⓇ), completelyto Mb, or no longer bindoxygen completely?Brief Explanation

The binding curve describes the relationship between the amount of oxygen bound to a molecule of…

Answered: D 1.0. 0.5- O 6. Answer the questions…

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

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
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?
2.1 ANSWER THE TABLE
. 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…
What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed values
pls solve this with in 1 hour

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