Issue 10, 2013

Microsecond folding experiments and simulations: a match is made

Abstract

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

Article information

Article type
Perspective
Submitted
09 נוב 2012
Accepted
16 ינו 2013
First published
29 ינו 2013

Phys. Chem. Chem. Phys., 2013,15, 3372-3388

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements