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Factors involved in the stability of isolated β-sheets: Turn sequence, β-sheet twisting, and hydrophobic surface burial
We have recently reported on the design of a 20-residue peptide able to form a significant population of a three-stranded up-and-down antiparallel β-sheet in aqueous solution. To improve our β-sheet model in terms of the folded population, we have modified the sequences of the two 2-residue turns by...
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| Autors principals: | , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Cold Spring Harbor Laboratory Press
2004
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2280049/ https://ncbi.nlm.nih.gov/pubmed/15044739 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.03520704 |
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