The relation between amino acid sequence and protein conformation |
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Authors: | D A Cook |
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Affiliation: | 3. Laboratory of Cellular and Structural Biology, Rockefeller University, New York, New York 10065;4. Departments of Biochemistry and of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461;5. New York Structural Biology Center, New York, New York 10027 |
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Abstract: | From studies of the amino acid sequence and conformation of myoglobin, human α- and β-haemoglobins and lysozyme, the following conclusions have been drawn: (a) that aspartic acid, glutamic acid and threonine occur preferentially at the N-terminal end of a helical segment, while lysine, arginine and histidine occur preferentially at the C-terminal end; (b) that alanine, valine and leucine tend to favour an α-helical conformation whereas asparagine, aspartic acid and phenylalanine have a “helix-breaking” effect; (c) that participation of hydrophobic amino acids in an α-helix is to some extent a function of side-chain size. |
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