Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature
Document Type
Article
Publication Date
2000
Abstract
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 opening for solvent access occurs in the ≃millisecond time frame or faster at 28°C for all amide positions. Under these conditions all backbone amides with exchange protection factors between 104 and 106, for which EX2 exchange kinetics were directly verified, have exchange activation energy values within 2-3 kcal/mol of that observed for unstructured peptides. The conformational flexibility of this protein is thus sufficient for water and base catalyst access to the exchanging amide with quite limited structural disruption. The common hypothesis that enhanced conformational rigidity in the folded native state underlies the increased thermal stability of hyperthermophile proteins is not supported by these data.
Publication Title
Proceedings of the National Academy of Sciences of the United States of America
Volume
97
Issue
7
First Page
3166
Last Page
3170
Recommended Citation
Hernandez, G. J.; Jenney, Francis E. Jr.; Adams, M. W.; and Lemaster, D. M., "Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature" (2000). PCOM Scholarly Works. 585.
https://digitalcommons.pcom.edu/scholarly_papers/585
Comments
This article was published in Proceedings of the National Academy of Sciences of the United States of America, Volume 97, Issue 7, Pages 3166-3170.
The published version is available at http://dx.doi.org/10.1073/pnas.040569697.Copyright © 2000 National Academy of Science.