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Conformational Analysis of Regular Enantiomeric Sequences
Abstract
Cylindrical coordinates and symmetries of regular enantiomeric sequences were derived on the basis of eigenvalue-eigenvectors solns. to the Eyring-transformation matrix, and were used to show that the general structure of conformationally equiv. enantiomers was a ring. Helical structures could be formed in the case of quasi-conformational equivalence between the monomeric units. For regular L,D copolypeptides, these helical structures were stabilized by both van der Waals and H bond interactions, and were more stable than the α-helix in the absence of configurational disorder.
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Citations
Cited by
Tesauro, D., Accardo, A., Diaferia, C., Milano, V., Guillon, J., Ronga, L., & Rossi, F. (2019) · Molecules · doi:10.3390/molecules24020351 · Cited by 225
Metadata
- Authors
- De Santis, P., Morosetti, S., & Rizzo, R.
- Venue
- Macromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 1974-01
- Volume
- 7
- Issue
- 1
- Pages
- 52-58
- ISSN
- 0024-9297 (ISSN-L)
- 1520-5835
- OpenAlex
- W1966666575
- Cited by
- 214
- References
- 0
- FWCI
- 0.57
- Type
- journal article
- Language
- en
- Open access
- closed
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- De Santis, P., Morosetti, S., & Rizzo, R. (1974). Conformational Analysis of Regular Enantiomeric Sequences. Macromolecules. https://doi.org/10.1021/ma60037a011
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.