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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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Bibliografiset tiedot
Päätekijät: Uzawa, Takanori, Akiyama, Shuji, Kimura, Tetsunari, Takahashi, Satoshi, Ishimori, Koichiro, Morishima, Isao, Fujisawa, Tetsuro
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 2004
Aiheet:
Linkit: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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