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Science 20 May 1994:
Vol. 264. no. 5162, pp. 1126 - 1130
DOI: 10.1126/science.8178170
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Articles

Science, Vol 264, Issue 5162, 1126-1130
Copyright © 1994 by American Association for the Advancement of Science

articles

Rules for alpha-helix termination by glycine

R Aurora, R Srinivasan, and GD Rose

Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.

A predictive rule for protein folding is presented that involves two recurrent glycine-based motifs that cap the carboxyl termini of alpha helices. In proteins, helices that terminated in glycine residues were found predominantly in one of these two motifs. These glycine structures had a characteristic pattern of polar and apolar residues. Visual inspection of known helical sequences was sufficient to distinguish the two motifs from each other and from internal glycines that fail to terminate helices. These glycine motifs--in which the local sequence selects between available structures--represent an example of a stereochemical rule for protein folding.


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