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Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of α-helical content and compactness

The characterization of protein folding dynamics in terms of secondary and tertiary structures is important in elucidating the features of intraprotein interactions that lead to specific folded structures. Apomyoglobin (apoMb), possessing seven helices termed A–E, G, and H in the native state, has a...

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Main Authors: Uzawa, Takanori, Akiyama, Shuji, Kimura, Tetsunari, Takahashi, Satoshi, Ishimori, Koichiro, Morishima, Isao, Fujisawa, Tetsuro
Formato: Artigo
Idioma:Inglês
Publicado: National Academy of Sciences 2004
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC337025/
https://ncbi.nlm.nih.gov/pubmed/14711991
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0305376101
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