Conformations of twisted parallel beta-sheets and the origin of chirality in protein structures
| Autor: | F R Salemme, D W Weatherford |
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| Rok vydání: | 1979 |
| Předmět: |
Models
Molecular Quantitative Biology::Biomolecules Multidisciplinary Optical Rotation Computers Protein Conformation Chemistry Hydrogen bond Beta sheet Hydrogen Bonding Crystallography Protein structure Physics::Space Physics Tetrahedron Peptide bond Twist Optical rotation Peptides Chirality (chemistry) Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 76:19-23 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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