| Literature DB >> 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.Entities:
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Year: 1979 PMID： 284331 PMCID： PMC382867 DOI： 10.1073/pnas.76.1.19
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205