Tryptophan zippers: Stable, monomeric β-hairpins
A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the β-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However,...
Αποθηκεύτηκε σε:
| Εκδόθηκε σε: | Proc Natl Acad Sci U S A |
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| Κύριοι συγγραφείς: | , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
2001
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC33255/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11331745/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.091100898 |
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