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Conformations of twisted parallel ( 3-sheets and the origin of chirality in protein structures ( secondary structure / protein chirality / hydrogen bond / peptide bond )
| Content Provider | Semantic Scholar |
|---|---|
| Author | Weatherford, Doris Salemme, F. R. |
| Abstract | An analysis of the conformational properties of parallel #-pleated sheets suggests that an important factor in the generation of ,-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 #-sheet structures with optimal hydrogen bond geometry. Crystallographic studies of proteins have revealed that many features of the secondary (1, 2) and supersecondary (3-5) structure of these molecules possess right-handed chirality. The results presented here, which treat the conformational properties of parallel fl-pleated sheets, suggest that nonplanar peptide bond distortions of preferred chirality may be an important factor in the generation of the observed handedness in protein structural domains. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.beta-sheet.org/resources/17-Conformations-of-Twisted....pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
