Millisecond Time Scale Conformational Flexibility in a Hyperthermophile Protein at Ambient Temperatu...
Millisecond Time Scale Conformational Flexibility in a Hyperthermophile Protein at Ambient Temperature
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United States: National Academy of Sciences of the United States of America
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Language
English
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United States: National Academy of Sciences of the United States of America
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Contents
Rubredoxin from the hyperthermophile Pyrococcus furiosus is the most thermostable protein characterized to date with an estimated global unfolding rate of 10-6s-1at 100 degrees C. In marked contrast to these slow global dynamics, hydrogen exchange experiments here demonstrate that conformational opening for solvent access occurs in the ≈ millisecon...
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Full title
Millisecond Time Scale Conformational Flexibility in a Hyperthermophile Protein at Ambient Temperature
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TN_cdi_proquest_journals_201386997
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201386997
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.97.7.3166
