Abstract
AbstractThe authors studied the temperature‐induced unfolding of ubiquitin by all‐atom Monte Carlo simulations. The unfolding behavior is compared with that seen in previous simulations of the mechanical unfolding of this protein, based on the same model. In mechanical unfolding, secondary‐structure elements were found to break in a quite well‐defined order. In thermal unfolding, the authors saw somewhat larger event‐to‐event fluctuations, but the unfolding pathway was still far from random. Two long‐lived secondary‐structure elements could be identified in the simulations. These two elements have been found experimentally to be the thermally most stable ones. Interestingly, one of these long‐lived elements, the first β‐hairpin, was found to break early in the mechanical unfolding simulations. Their combined simulation results thus enable the authors to predict in detail important differences between the thermal and mechanical unfolding behaviors of ubiquitin. Proteins 2006. © 2006 Wiley‐Liss, Inc.
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Dates
Type | When |
---|---|
Created | 18 years, 11 months ago (Sept. 5, 2006, 6:51 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 28, 2023, 9:21 p.m.) |
Indexed | 6 months, 1 week ago (Feb. 21, 2025, 6:53 a.m.) |
Issued | 18 years, 11 months ago (Sept. 5, 2006) |
Published | 18 years, 11 months ago (Sept. 5, 2006) |
Published Online | 18 years, 11 months ago (Sept. 5, 2006) |
Published Print | 18 years, 9 months ago (Nov. 15, 2006) |
Funders
1
Swedish Research Council
10.13039/501100004359
VetenskapsrådetRegion: Europe
gov (National government)
Labels
2
- Swedish Research Council
- VR
@article{Irb_ck_2006, title={Thermal versus mechanical unfolding of ubiquitin}, volume={65}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.21145}, DOI={10.1002/prot.21145}, number={3}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Irbäck, Anders and Mitternacht, Simon}, year={2006}, month=sep, pages={759–766} }