A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate animals) is shown to
Question:
a. It has been found that in some of the α-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?
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a The four helices could be arranged so that the hydrophobic side chains wo...View the full answer
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Related Book For
Biochemistry Concepts and Connections
ISBN: 978-0321839923
1st edition
Authors: Dean R. Appling, Spencer J. Anthony Cahill, Christopher K. Mathews
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