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Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin

Characterization of the conformational landscapes for proteins with different secondary structures is important in elucidating the mechanism of protein folding. The folding trajectory of single-chain monellin composed of a five-stranded β-sheet and a helix was investigated by using a pH-jump from th...

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Detalhes bibliográficos
Main Authors: Kimura, Tetsunari, Uzawa, Takanori, Ishimori, Koichiro, Morishima, Isao, Takahashi, Satoshi, Konno, Takashi, Akiyama, Shuji, Fujisawa, Tetsuro
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2005
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC549438/
https://ncbi.nlm.nih.gov/pubmed/15710881
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0407982102
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