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. 1973 Feb;70(2):538–542. doi: 10.1073/pnas.70.2.538

The Reverse Turn as a Polypeptide Conformation in Globular Proteins

James L Crawford *, William N Lipscomb *, Charlotte G Schellman *
PMCID: PMC433301  PMID: 4510294

Abstract

The reverse turn, involving four consecutive amino acids, as a tertiary conformation in globular proteins is defined in terms of dihedral angles, the C1α...C4α distance and the O1...H-N4 hydrogen bond distance. In seven proteins we find 125 examples of turns, comprising 33% of the amino acids in these proteins, as compared with 34% of the residues forming helices and only 17% forming β-sheets. The amino-acid compositions of turns, helices, and β-sheets are analyzed in some detail. We find Asn and Gly mainly in turns, Pro in turns (and at the beginning of helices), and Glu in helices. In these turns a statistical survey indicates that 19% of Asp residues are in the first position, 33% of Pro residues are in the second position, 24% of Asn residues are in the third position, and 26% of Trp residues are in the fourth position.

Keywords: amino-acid composition, helices, β-sheets

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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