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Amino acid intrinsic α-helical propensities III: Positional dependence at several positions of C terminus
In this study, we have analyzed experimentally the helical intrinsic propensities of noncharged and nonaromatic residues at different C-terminal positions (C1, C2, C3) of an Ala-based peptide. The effect was found to be complex, resulting in extra stabilization or destabilization, depending on guest...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2002
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2373540/ https://ncbi.nlm.nih.gov/pubmed/11910021 |
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