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

Publicado no:	Proc Natl Acad Sci U S A
Principais autores:	Hernández, Griselda, Jenney, Francis E., Adams, Michael W. W., LeMaster, David M.
Formato:	Artigo
Idioma:	Inglês
Publicado em:	National Academy of Sciences 2000
Assuntos:	Biological Sciences
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC16210/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10716696/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.040569697
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