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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Bibliographic Details
Main Authors: Uzawa, Takanori, Akiyama, Shuji, Kimura, Tetsunari, Takahashi, Satoshi, Ishimori, Koichiro, Morishima, Isao, Fujisawa, Tetsuro
Format: Artigo
Language:Inglês
Published: National Academy of Sciences 2004
Subjects:
Biological Sciences
Online Access: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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