Effect of side chain-backbone electrostatic interactions on the stability of alpha-helices.
An apparent discrepancy between the observed stability of the C-peptide alpha-helix of ribonuclease A and that computed from the Zimm-Bragg parameters sigma and s (obtained by the host-guest technique) is resolved. Side chain-backbone ion-dipole interactions play a role in both systems. However, the...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autor: | |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1985
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC390595/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3862082/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.82.17.5585 |
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