A diagram of the residues defining the binding site of 2,3-bis-phosphoglycerate (BPG) is2. (shown on the right. Given the mutation in Hb Great Lakes, Leu(B68)His, show on either O2 binding plotwhether its p(O2)50% will be altered in the presence of a 10-fold excess of BPG and in which directionwith respect to that of HbA. Explain.B1B1-subunitHis 143Lys82His 2BPGa-NH,*a-NH,*B2-subunitLys 82His 2His 143B2

2,3 bis phosphoglycerate (BPG) is an allosteric regulator of Hb. BPG binds to central cavity of…

Answered: 2. (: A diagram of the residues…

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

5. (a) Hexokinase IV is known as glucokinase (GCK) and is a central metabolic enzyme that participates in glucose homeostatic maintenance by governing the rates of glucose catabolism in pan- creatic B-cells and glycogen storage in hepatocytes (liver cells). In contrast to the regulatory mecha- nisms of hexokinase I or Il in other tissues, GCk is regulated by binding to the Glucokinase Regulatory Protein (GRP) located in the cell nucleus. When glucose in hepatocytes is low, GCK is sequestered in the nucleus by binding to the GRP. High glucose, for instance, after ingestion of a meal, disrupts the GRP-GCK complex, allowing the GCK to diffuse into the cytoplasm to convert glucose into glucose-6- phosphate. Contrast the properties of hexokinases I and IV with respect to oligomeric structure, mech- anism of regulation of their activity, KM value, and dependence of catalytic activity on cellular location. Hexokinase l is found in, for instance, muscle tissue. Property subunit structutre…
10. In an abnormal hemoglobin variant known as Hemoglobin-Kariya, the lysine residues at position 40 in the ß-chains are replaced by glutamic acid residues. a) What effect would you expect this change to have on the quaternary structure and oxygen binding properties of hemoglobin? b) Draw a diagram to illustrate the difference in the oxygen binding curves that would be obtained with normal hemoglobin and Hemoglobin-Kariya.
1.Substituents exhibit strong steric repulsion at the GABAA receptor ？what does it means？？ 2. Substitutions at C-6, C-8, and C-9 lower the activity？where is C-6, C-8, and C-9 ？can anyone help to lable out？
Compare and contrast the c4 pathway and the malate–aspartate shuttle in bullet format, meaning list the similarities and differences.
Some are unable to taste thiourea and PTC. DNA sequence results for these individuals show a normal predicted amino acid sequence for the TAS2R38 gene. Provide an explanation that can account for insensitivity to thiourea. (a) First assuming a mutation involving the TAS2R38 gene (b) Then assuming a mutation in a gene other than TAS2R38
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate. Which of the following are true for the protein, ATP synthase? Select all apply A mutation of Asp61 to glutamic acid would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to alanine A mutation of Asp61 to alanine would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to glutamic acid The F1 subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis The FO subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis
The action of this enzyme found in Beano alpha-galactosidase can also according to many sources be used to remove ____________ from the red blood cells of the B blood group and convert them to the O blood group. Since the _________ molecules (composed of many monomers) are connnected to protein on the membrane and also the cell membrane of the red blood cell itself; therefore these molecules help create cell identity and recognition, and when the are connected to proteins they are known as _________ , but if they are connected to the cell membrane itself they are known as ____________. This is a good question for reviewing the structures on the cell membrane as well. The only difference between the B-blood type and the O-blood type is ________. The following is a diagram of the differences of these molecules that determine blood type. List of answers: disaccharid, proteins ,dehydration synthesis ,nucleotide ,amino acids ,nucleic acids ,lactose ,fructose ,sucrose ,hydrolysis…
2. The diagram to the right shows the change in the structure of the C-terminal portion of each of the ẞ-subu- nits of human hemoglobin (HbA) in the oxyHb to deox- yHb or R-to-T transition. The hydrogen bonding interac- tion of the C-terminal ẞHis 146 residue with the side chain of Asp94, highlighted by the red ellipse, has been shown to be responsible for a major portion of the proton uptake associated with the Bohr effect. Treatment of HbA with the enzyme carboxypeptidase A (CPA) results in loss of the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ- subunits. (a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y = fraction of heme groups occupied by O2] to compare the values of the Hill coefficient nн and the O2-binding affinity at pH 7.4 of normal HbA before and after treat- ment of with CPA. (b) (' ) How will the plot for CPA-digested HbA change at pH 7.2? (c) 1 Hi5146 HN- ✓ Low PK B-chain. CH2 CH-NH-CO-CH-NH- CH₂ Tyr145 он HbO2 or R state Туг145 CH-CH2- OH co NH CH CH₂ His…
The enzymatic activity of PFK1 is generally measured by set- ting up a coupled enzyme assay system whereby aldolase, triose phos- phate isomerase, and glycerol-3-phosphate dehydrogenase are added to the assay mixture. For the latter enzyme, NADH is added and its change in concentration is readily monitored at 340 nm. Write the chain of reactions catalyzed by these enzymes using structural formulas, label substrates and products, and explain why the coupled en- zyme assay system leads to oxidation of NADH. While the chain of reac- tions is similar to those in glycolysis, there is a critical difference because of the dehydrogenase enzyme. Describe how this enzyme causes the chain of reactions to differ from those in glycolysis.
Could you please help answer this question?
The ABO blood group antigens are the terminal sugars covalently linked to the end of the glycolipid in the red blood cellmembrane. The H antigen is the precursor of the A and Bantigens. Individuals with type A blood produce a gene thatcodes for an enzyme that adds N-acetylgalactosamine in ana(1,3) linkage to the Gal* residue in the H antigen. Type Bblood requires that an enzyme add a d-a galactose in an a(1,3) linkage to the Gal*. Draw the structures of the A andB antigens.
PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?

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