1. In fetal hemoglobin, residue 143 of the beta subunit is a serine rather than the histidine found in adult hemoglobin (see figure on page 9). a) What does this do to the charges in the BPG binding cavity? b) Would you expect this to change the oxygen affinity of fetal hemoglobin, and, if so, in what direction?

1. In fetal hemoglobin, residue 143 of the beta subunit is a serine rather than the histidine found in adult hemoglobin (see figure on page 9). a) What does this do to the charges in the BPG binding cavity? b) Would you expect this to change the oxygen affinity of fetal hemoglobin, and, if so, in what direction?

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Description: 1. In fetal hemoglobin, residue 143 of the beta subunit is a serine rather than the histidine foundin adult hemoglobin (see figure on page 9).a) What does this do to the charges in the BPG binding cavity?b) Would you expect this to change the oxygen

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 20QP: If an extra nucleotide is inserted in the first exon of the beta globin gene, what effect will it...

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Please fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to the
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