Interior turns in globular proteins

George D Rose, William B. Young, Lila M. Gierasch

Research output: Contribution to journalArticle

Abstract

Reverse turns are specific sites in proteins at which the polypeptide chain changes its overall direction1-6. This category of secondary structure enables the chain to turn a corner, and its frequent occurrence 7,8 is the geometric basis for the ultimate globular shape of the protein. β-Turns in particular are comprised of four consecutive residues with a stereochemistry9 that constrains the turn to be polar. In consequence, turns are almost always situated at the surface of the protein, in contact with solvent water. We have searched proteins of known structure and find that, on occasion, a turn may be buried within the hydrophobic interior of the molecule. In every instance of a buried turn, one or more solvent molecules were also found in a hydrogen-bonded complex with main-chain atoms of the turn residues. These bound water molecules appear to function as an integral part of the protein structure.

Original languageEnglish (US)
Pages (from-to)654-657
Number of pages4
JournalNature
Volume304
Issue number5927
DOIs
StatePublished - 1983
Externally publishedYes

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Proteins
Water
Hydrogen
Membrane Proteins
Peptides

ASJC Scopus subject areas

  • General

Cite this

Rose, G. D., Young, W. B., & Gierasch, L. M. (1983). Interior turns in globular proteins. Nature, 304(5927), 654-657. https://doi.org/10.1038/304654a0

Interior turns in globular proteins. / Rose, George D; Young, William B.; Gierasch, Lila M.

In: Nature, Vol. 304, No. 5927, 1983, p. 654-657.

Research output: Contribution to journalArticle

Rose, GD, Young, WB & Gierasch, LM 1983, 'Interior turns in globular proteins', Nature, vol. 304, no. 5927, pp. 654-657. https://doi.org/10.1038/304654a0
Rose, George D ; Young, William B. ; Gierasch, Lila M. / Interior turns in globular proteins. In: Nature. 1983 ; Vol. 304, No. 5927. pp. 654-657.
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