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Issue 10, 2013
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Microsecond folding experiments and simulations: a match is made

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For the past two decades, protein folding experiments have been speeding up from the second or millisecond time scale to the microsecond time scale, and full-atom simulations have been extended from the nanosecond to the microsecond and even millisecond time scale. Where the two meet, it is now possible to compare results directly, allowing force fields to be validated and refined, and allowing experimental data to be interpreted in atomistic detail. In this perspective we compare recent experiments and simulations on the microsecond time scale, pointing out the progress that has been made in determining native structures from physics-based simulations, refining experiments and simulations to provide more quantitative underlying mechanisms, and tackling the problems of multiple reaction coordinates, downhill folding, and complex underlying structure of unfolded or misfolded states.

Graphical abstract: Microsecond folding experiments and simulations: a match is made

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Publication details

The article was received on 09 Nov 2012, accepted on 16 Jan 2013 and first published on 29 Jan 2013

Article type: Perspective
DOI: 10.1039/C3CP43992E
Phys. Chem. Chem. Phys., 2013,15, 3372-3388

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    Microsecond folding experiments and simulations: a match is made

    M. B. Prigozhin and M. Gruebele, Phys. Chem. Chem. Phys., 2013, 15, 3372
    DOI: 10.1039/C3CP43992E

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