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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...

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Detalhes bibliográficos
Main Authors: Ihalainen, Janne A., Paoli, Beatrice, Muff, Stefanie, Backus, Ellen H. G., Bredenbeck, Jens, Woolley, G. Andrew, Caflisch, Amedeo, Hamm, Peter
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2008
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Acesso em linha: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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