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PMID: 3381086 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Science (New York, N.Y.) ·Vol. 240 ·No. 4859 ·1988-06-17 ·Pages 1648-52

Richardson JS, Richardson DC

Abstract

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.

MeSH Terms
Amino Acid Sequence Amino Acids Asparagine Hydrogen Bonding Proline Protein Conformation
Chemicals
Amino Acids Asparagine Proline
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Richardson J S
Department of Biochemistry, Duke University, Durham, NC 27710.
Richardson D C
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1988-06-17
Pages
1648-52
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM-15000 · United States
Corrections
ErratumIn
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