1. Which of the following statements is trueabout the functional role of His E7 inhemoglobin?a. For hemoglobin, His E7's sidechain H-bond to O₂ increases the preference for O2binding to the heme group; however, CObinding is still favored.b. Under acidic conditions His E7 isprotonated and forms a salt bridge withAsp FG1 to lock hemoglobin in the "T-state".c. His E7 has a free carboxylic acid terminusthat forms a carbamino adduct with CO2.This is the molecular cause of the "BohrEffect".

His- E7, which is thought to stabilize bound O2 by hydrogen bonding and inhibit CO in hemoglobin .

Which of the following statements is true about the functional role of His E7 in hemoglobin? a. For hemoglobin, His E7's sidechain H- pond to O2 increases the preference for O2 binding to the heme group; however, CO binding is still favored. o. Under acidic conditions His E7 is protonated and forms a salt bridge with Asp FG1 to lock hemoglobin in the "T-state". C. His E7 has a free carboxylic acid terminus hat forms a carbamino adduct with CO2. This is the molecular cause of the "Bohr Effect".

Which of the following statements is true about the functional role of His E7 in hemoglobin? a. For hemoglobin, His E7's sidechain H- pond to O2 increases the preference for O2 binding to the heme group; however, CO binding is still favored. o. Under acidic conditions His E7 is protonated and forms a salt bridge with Asp FG1 to lock hemoglobin in the "T-state". C. His E7 has a free carboxylic acid terminus hat forms a carbamino adduct with CO2. This is the molecular cause of the "Bohr Effect".

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

b) The methyl group at the C terminus of aspartame can be cleaved by concentrated sulfuric acid (conc. H₂SO4) to reveal the carboxylic acid (compound 1), which has a pK₂ of 2.43. OH NH₂ OCH3 conc. H₂SO4 OH NH₂ OH Compound 1 The other two pKa values in the molecule are unchanged. It is useful to calculate the isoelectric point (pl) when planning to separate charged species from neutral species with electrophoresis. pKal + PK₂2 2 pl = HINT: i) Calculate the isoelectric point of aspartame. ii) Calculate the isoelectric point of compound 1 and explain your reasoning behind the calculation.
Consider the decapeptide angiotensin I. What products are formed when angiotensin I is treated withchymotrypsin?
Chemistry Given TETRAPEPTIDE: Prolinyl-Argininyl-Cysteinyl-Tryptophan Predict the direction of the peptide in electrophoresis at pH 7 and pH11.5. (Use table on the upper right for the estimated pK values of some functional groups).
*In the presence of saturating amounts of oxaloacetate, the activity of citrate synthase from pig heart tissue shows a sigmoidal dependence on the concentration of acetyl-SCOA as shown below. SCOA is added, the curve shifts to the right and becomes even more sigmoidal. On the basis of these observations, explain how succinyl- SCOA regulates the activity of citrate synthase. Why is succinyl-SCOA an appropriate signal for regulation of the citric acid cycle? does the regulation of citrate synthase control the rate of cellular respiration in pig heart tissue? 100 - 80 succinyl-CoA Activity (% of V, 60 40- No Succinyl-CoA added 20 40 60 80 100 120 [Acetyl-CoAl(pM) - How -
Which of the following statements could be considered true for both the Hsp70-mediated and GroEL- GroES-mediated protein-folding processes? Choose one: ADP hydrolysis is critical to completion of the protein-folding cycle. Both Hsp70 and GroEL-GroES are considered chamber-type chaperones. Proteins are typically released from both complexes in a partially folded form and the folding cycle may need to be repeated multiple times. Exposed hydrophilic patches on the surface of unfolded proteins initiate recognition with chaperones.
e begin you jest gee OH of al. big the end OH leflaver B corbony! group IR 14.14 3. Nature uses nicotinamide adenine dinucleotide NAD+) to oxidize alcohols. It is a Teversible process. What IR bands would vou want to follow if you needed to monitor this biochemical process? Explain why this would work. NAD* + NADH H.
Give all the answer just with small explanation Asap Thanks
5
Carboxypeptidase requires a Zn²+ cofactor for the hydrolysis of the peptide bond of a C-terminal aromatic amino acid. T/F This is a structure of vitamin A. Is it polar or non polar? Explain OH
Short answer 5-6 lines.
Carboxypeptidase requires a Zn²+ cofactor for the hydrolysis of the peptide bond of a C-terminal aromatic amino acid. T/F?
Which of the following statements is false concerning the structure of hemoglobin? O The R-state of Hb is favored under environments of high concentrations of O2 The binding of BPG stabilizes the low affinity state of Hb O Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons Hemoglobin's affinity for oxygen increases in the presence of carbamates O Hemoglobin favors the R-state in basic environments