Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 31, Problem 20P
Interpretation Introduction
Interpretation:
A 20 residue long amino acid sequence needs to be designed that results in the amphipathic alpha-helical secondary structure.
Concept Introduction :
The AH or membrane-binding amphipathic helix is a communal motif encountered in numerous peptides and proteins. Amphipathicity resembles to the separation of polar and hydrophobic residues between the two opposite faces of the a-helix, a distribution designed for the membrane binding.
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Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?
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