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Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR

The earliest steps in the folding of proteins are complete on an extremely rapid time scale that is difficult to access experimentally. We have used rapid-mixing quench-flow methods to extend the time resolution of folding studies on apomyoglobin and elucidate the structural and dynamic features of...

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מידע ביבליוגרפי
Main Authors: Uzawa, Takanori, Nishimura, Chiaki, Akiyama, Shuji, Ishimori, Koichiro, Takahashi, Satoshi, Dyson, H. Jane, Wright, Peter E.
פורמט: Artigo
שפה:Inglês
יצא לאור: National Academy of Sciences 2008
נושאים:
גישה מקוונת:https://ncbi.nlm.nih.gov/pmc/articles/PMC2544544/
https://ncbi.nlm.nih.gov/pubmed/18779573
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0804033105
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