i. A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate animals) is shown to the right. (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?
i. A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate animals) is shown to the right. (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?
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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![i. A schematic structure of the subunit of hemerythrin (an oxygen-binding
protein from invertebrate animals) is shown to the right.
(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?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fe9026865-cc79-4dcd-b783-f75f68fc422f%2F10161f8c-5262-4073-818b-7d85183eb1d6%2Fkhf3rrfj_processed.png&w=3840&q=75)
Transcribed Image Text:i. A schematic structure of the subunit of hemerythrin (an oxygen-binding
protein from invertebrate animals) is shown to the right.
(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?
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