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PMID: 7756980 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A revised set of potentials for beta-turn formation in proteins.

Protein science : a publication of the Protein Society ·Vol. 3 ·No. 12 ·1994-12-00 ·Pages 2207-16

Hutchinson EG, Thornton JM

Abstract

Three thousand eight hundred ninety-nine beta-turns have been identified and classified using a nonhomologous data set of 205 protein chains. These were used to derive beta-turn positional potentials for turn types I' and II' for the first time and to provide updated potentials for formation of the more common types I, II, and VIII. Many of the sequence preferences for each of the 4 positions in turns can be rationalized in terms of the formation of stabilizing hydrogen bonds, preferences for amino acids to adopt a particular conformation in phi, psi space, and the involvement of turn types I' and II' in beta-hairpins. Only 1,632 (42%) of the turns occur in isolation; the remainder have at least 1 residue in common with another turn and have hence been classified as multiple turns. Several types of multiple turn have been identified and analyzed.

MeSH Terms
Amino Acids/chemistry Chemical Phenomena Chemistry, Physical Hydrogen Bonding Protein Structure, Secondary
Chemicals
Amino Acids
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hutchinson E G
Department of Biochemistry and Molecular Biology, University College, London, United Kingdom.
Thornton J M
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
Published
1994-12-00
Pages
2207-16
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2142776
Subset
IM
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