Thermal versus mechanical unfolding of ubiquitin

Anders Irbäck, Simon Mitternacht

    Research output: Contribution to journalArticlepeer-review

    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.
    Original languageEnglish
    Pages (from-to)759-766
    JournalProteins
    Volume65
    Issue number3
    DOIs
    Publication statusPublished - 2006

    Subject classification (UKÄ)

    • Biophysics

    Free keywords

    • protein folding
    • unfolding
    • temperature-induced unfolding
    • all-atom model
    • force-induced
    • Monte Carlo simulation

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