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Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature

Rubredoxin from the hyperthermophile Pyrococcus furiosus is the most thermostable protein characterized to date with an estimated global unfolding rate of 10(−6) s(−1) at 100°C. In marked contrast to these slow global dynamics, hydrogen exchange experiments here demonstrate that conformational openi...

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Detalhes bibliográficos
Main Authors: Hernández, Griselda, Jenney, Francis E., Adams, Michael W. W., LeMaster, David M.
Formato: Artigo
Idioma:Inglês
Publicado em: The National Academy of Sciences 2000
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC16210/
https://ncbi.nlm.nih.gov/pubmed/10716696
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