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Science 17 June 1988:
Vol. 240. no. 4859, pp. 1648 - 1652
DOI: 10.1126/science.3381086

Articles

Science, Vol 240, Issue 4859, 1648-1652
Copyright © 1988 by American Association for the Advancement of Science


articles

Amino acid preferences for specific locations at the ends of alpha helices

JS Richardson and DC Richardson

Department of Biochemistry, Duke University, Durham, NC 27710.

A definition based on alpha-carbon positions and a sample of 215 alpha helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.


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The Crystal Structure of Indoleglycerol-phosphate Synthase from Thermotoga maritima. KINETIC STABILIZATION BY SALT BRIDGES.
T. Knochel, A. Pappenberger, J. N. Jansonius, and K. Kirschner (2002)
J. Biol. Chem. 277, 8626-8634
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Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha -helices.
S. T. Thomas, V. V. Loladze, and G. I. Makhatadze (2001)
PNAS 98, 10670-10675
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Science. ISSN 0036-8075 (print), 1095-9203 (online)