Biochemistry: Concepts and Connections (2nd Edition)
Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 6, Problem 3P

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?

Chapter 6, Problem 3P, A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate

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Eukaryotic protein X has one proline residue and two cysteine residues. The proline needs to be in the cis-configuration in the folding protein; and a disulphide bond is formed between the cysteines in the folded protein. Discuss the folding of the protein in solution with protein disulphide isomerase and peptidyl-prolyl isomerase and without these enzymes. Use illustrations to show the differences in the potential folding of protein X under the different conditions.
In the molecule of oligomeric protein there are 19 lysine residues. 12 of them may be easily acetylated with anhydrides of dicarbon acids (it react with NH2-groups). The acetylation of extra two residues of lysine will dissociate the protein to the subunits. The rest 5 lysine residues may be modified only after denaturation of the protein. Suggest, how many lysine residues are: a) on a surface of protein globule; b) inside globule: c) in a site which is responsible for the contact within subunits
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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Mitochondrial mutations; Author: Useful Genetics;https://www.youtube.com/watch?v=GvgXe-3RJeU;License: CC-BY