Thermal versus mechanical unfolding of ubiquitin

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Thermal versus mechanical unfolding of ubiquitin. / Irbäck, Anders; Mitternacht, Simon.

In: Proteins, Vol. 65, No. 3, 2006, p. 759-766.

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Irbäck, Anders ; Mitternacht, Simon. / Thermal versus mechanical unfolding of ubiquitin. In: Proteins. 2006 ; Vol. 65, No. 3. pp. 759-766.

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TY - JOUR

T1 - Thermal versus mechanical unfolding of ubiquitin

AU - Irbäck, Anders

AU - Mitternacht, Simon

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - protein folding

KW - unfolding

KW - temperature-induced unfolding

KW - all-atom model

KW - force-induced

KW - Monte Carlo simulation

U2 - 10.1002/prot.21145

DO - 10.1002/prot.21145

M3 - Article

VL - 65

SP - 759

EP - 766

JO - Proteins

T2 - Proteins

JF - Proteins

SN - 0887-3585

IS - 3

ER -