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Fetal hemoglobin comprises of ay sub-units. It has been found that the y-chain contains serine at position 143 instead of Histidine 143 normally found in the B-chain. The amino acid 143 lines the DPG binding site. This mutation in the y chain results in O Increased DPG binding in the fetal hemoglobin Increased efficiency of oxygen transport to the lungs in the fetus. O Increased Oxygen binding in the fetus. O This is a silent mutation, L.e. no change should be observed. QUESTION 2 pH>7 in the lungs results in O deprotonating of histidine, making it negatively charged. O protonating of histidine, making it neutral. O deprotonating of histidine, making it neutral. protonating of histidine, making it positively charged.

Fetal hemoglobin comprises of ay sub-units. It has been found that the y-chain contains serine at position 143 instead of Histidine 143 normally found in the B-chain. The amino acid 143 lines the DPG binding site. This mutation in the y chain results in O Increased DPG binding in the fetal hemoglobin Increased efficiency of oxygen transport to the lungs in the fetus. O Increased Oxygen binding in the fetus. O This is a silent mutation, L.e. no change should be observed. QUESTION 2 pH>7 in the lungs results in O deprotonating of histidine, making it negatively charged. O protonating of histidine, making it neutral. O deprotonating of histidine, making it neutral. protonating of histidine, making it positively charged.

Chemistry
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...
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can you check my questions 1,2 and 4! and help me with 3
QUESTION 3 The disruption of which of the following interactions directly contributes towards removing 2,3-BPG from HB? O Tyr 145-Val 98 O His 146-Asp 94 His 146-Lys 40 O Tyr-145-His 146 QUESTION 4 In sickle cell anemia, hemoglobin forms long fibers as a result of O Exposing polar amino acids Electrostatic interaction between glutamate and non polar amino acids O Burying polar amino acids Burying of non-polar amino acids
Transcribed Image Text:QUESTION 3 The disruption of which of the following interactions directly contributes towards removing 2,3-BPG from HB? O Tyr 145-Val 98 O His 146-Asp 94 His 146-Lys 40 O Tyr-145-His 146 QUESTION 4 In sickle cell anemia, hemoglobin forms long fibers as a result of O Exposing polar amino acids Electrostatic interaction between glutamate and non polar amino acids O Burying polar amino acids Burying of non-polar amino acids
Fetal hemoglobin comprises of ay sub-units. It has been found that the y-chain contains serine at position 143 instead of Histidine 143 normally found in the B-chain. The amino acid 143 lines the DPG binding site. This mutation in the y chain results in O Increased DPG binding in the fetal hemoglobin Increased efficiency of oxygen transport to the lungs in the fetus. O Increased Oxygen binding in the fetus. O This is a silent mutation, i.e. no change should be observed. QUESTION 2 pH>7 in the lungs results in O deprotonating of histidine, making it negatively charged. O protonating of histidine, making it neutral. O deprotonating of histidine, making it neutral. protonating of histidine, making it positively charged.
Transcribed Image Text:Fetal hemoglobin comprises of ay sub-units. It has been found that the y-chain contains serine at position 143 instead of Histidine 143 normally found in the B-chain. The amino acid 143 lines the DPG binding site. This mutation in the y chain results in O Increased DPG binding in the fetal hemoglobin Increased efficiency of oxygen transport to the lungs in the fetus. O Increased Oxygen binding in the fetus. O This is a silent mutation, i.e. no change should be observed. QUESTION 2 pH>7 in the lungs results in O deprotonating of histidine, making it negatively charged. O protonating of histidine, making it neutral. O deprotonating of histidine, making it neutral. protonating of histidine, making it positively charged.
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