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

D.W. Weatherford | Zendy; F.R. Salemme | Zendy

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

Author(s) -

D.W. Weatherford,

F.R. Salemme

Publication year - 1979

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.76.1.19

Subject(s) - beta sheet , twist , chirality (physics) , crystallography , beta (programming language) , hydrogen bond , tetrahedron , peptide , protein structure , chemistry , deformation (meteorology) , character (mathematics) , stereochemistry , materials science , physics , geometry , molecule , mathematics , chiral symmetry , biochemistry , organic chemistry , quantum mechanics , computer science , nambu–jona lasinio model , programming language , quark , composite material

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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