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. 1979 Jan;76(1):19–23. doi: 10.1073/pnas.76.1.19

Conformations of twisted parallel beta-sheets and the origin of chirality in protein structures.

D W Weatherford, F R Salemme
PMCID: PMC382867  PMID: 284331

Abstract

An analysis of the conformational properties of parallel beta-pleated sheets suggests that an important factor in the generation of beta-sheet twist is the preference for nonplanar peptide bond distortions that impart local left-handed helical character to polypeptide chains. It is demonstrated that the introduction of such chiral distortions, which result from the tetrahedral deformation of the peptide nitrogen atoms, naturally produces right-twisted beta-sheet structures with optimal hydrogen bond geometry.

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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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