Biology
Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 15.1, Problem 1CC

Consequences of Mutations

Concept Check: Based on the fiber-like structures seen in part (c) of this figure, what aspect of hemoglobin structure does a glutamic acid at the sixth position in normal β-globin prevent? Speculate as to how the charge of this amino acid may play a role.

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Suggest probable consequences of the following real or possible hemoglobinmutations. [Note: as shown](a) At β146 (HC3) His → Asp(b) At β92 (F8) His → LeuIn each case, indicate whether a single-nucleotide change is sufficient forthe mutation.
-. A schematic structure of the subunit of hemerythrin (an oxygen- binding protein from invertebrate animals) is shown below. (a) It has been found that in some of the a-helical regions of hemerythrin, about every third or fourth amino acid residue is a hydrophobic one. Suggest a structural reason for this finding. (b) What would be the effect of a mutation that placed a proline residue at point A in the structure? A Fe
Myoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.
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Mitochondrial mutations; Author: Useful Genetics;https://www.youtube.com/watch?v=GvgXe-3RJeU;License: CC-BY