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Thermal versus mechanical unfolding of ubiquitin

Irbäck, Anders LU and Mitternacht, Simon LU (2006) In Proteins 65(3). p.759-766
Abstract
The 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 P-hairpin, was found to... (More)
The 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 P-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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
protein folding, unfolding, temperature-induced unfolding, all-atom model, force-induced, Monte Carlo simulation
in
Proteins
volume
65
issue
3
pages
759 - 766
publisher
John Wiley & Sons
external identifiers
  • wos:000241247100020
  • scopus:33750073182
ISSN
0887-3585
DOI
10.1002/prot.21145
language
English
LU publication?
yes
id
bca98733-504e-477c-a600-077c28920e86 (old id 387275)
date added to LUP
2007-10-05 12:51:51
date last changed
2019-08-28 03:09:07
@article{bca98733-504e-477c-a600-077c28920e86,
  abstract     = {The 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 P-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.},
  author       = {Irbäck, Anders and Mitternacht, Simon},
  issn         = {0887-3585},
  keyword      = {protein folding,unfolding,temperature-induced unfolding,all-atom model,force-induced,Monte Carlo simulation},
  language     = {eng},
  number       = {3},
  pages        = {759--766},
  publisher    = {John Wiley & Sons},
  series       = {Proteins},
  title        = {Thermal versus mechanical unfolding of ubiquitin},
  url          = {http://dx.doi.org/10.1002/prot.21145},
  volume       = {65},
  year         = {2006},
}