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Open Biol. 2012 Jul;2(7):120087. doi: 10.1098/rsob.120087.

Accelerated simulation of unfolding and refolding of a large single chain globular protein.

Author information

1
Adelard Institute, Manchester M29 7FZ , UK.

Abstract

We have developed novel strategies for contracting simulation times in protein dynamics that enable us to study a complex protein with molecular weight in excess of 34 kDa. Starting from a crystal structure, we produce unfolded and then refolded states for the protein. We then compare these quantitatively using both established and new metrics for protein structure and quality checking. These include use of the programs Concoord and Darvols. Simulation of protein-folded structure well beyond the molten globule state and then recovery back to the folded state is itself new, and our results throw new light on the protein-folding process. We accomplish this using a novel cooling protocol developed for this work.

KEYWORDS:

enzyme reactivation; molecular dynamics; protein folding; protein structure

PMID:
22870389
PMCID:
PMC3411113
DOI:
10.1098/rsob.120087
[Indexed for MEDLINE]
Free PMC Article

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