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α-Helix folding in the presence of structural constraints
We have investigated the site-specific folding kinetics of a photoswitchable cross-linked α-helical peptide by using single (13)C = (18)O isotope labeling together with time-resolved IR spectroscopy. We observe that the folding times differ from site to site by a factor of eight at low temperatures...
Tallennettuna:
| Päätekijät: | , , , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2008
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2474473/ https://ncbi.nlm.nih.gov/pubmed/18621686 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0712099105 |
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