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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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| Main Authors: | , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
The National Academy of Sciences
2000
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC16210/ https://ncbi.nlm.nih.gov/pubmed/10716696 |
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