Atomistic protein folding simulations on the submillisecond time scale using worldwide distributed computing

Atomistic simulations of protein folding have the potential to be a great complement to experimental studies, but have been severely limited by the time scales accessible with current computer hardware and algorithms. By employing a worldwide distributed computing network of tens of thousands of PCs...

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Bibliographic Details
Published in:Biopolymers 2003-01, Vol.68 (1), p.91-109
Main Authors: Pande, Vijay S., Baker, Ian, Chapman, Jarrod, Elmer, Sidney P., Khaliq, Siraj, Larson, Stefan M., Rhee, Young Min, Shirts, Michael R., Snow, Christopher D., Sorin, Eric J., Zagrovic, Bojan
Format: Article
Language:English
Subjects:
Algorithms
atomistic protein folding
beta hairpin
Carrier Proteins - chemistry
computer algorithms
computer hardware
Computer Simulation
distributed computing
Kinetics
Microfilament Proteins - chemistry
microsecond time scale
Models, Chemical
Models, Molecular
molecular dynamics
Nerve Tissue Proteins - chemistry
Protein Folding
Protein Structure, Secondary
Proteins - chemistry
Proteins - metabolism
Reproducibility of Results
Solvents
Thermodynamics
Time Factors
villin
Viscosity
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Summary:Atomistic simulations of protein folding have the potential to be a great complement to experimental studies, but have been severely limited by the time scales accessible with current computer hardware and algorithms. By employing a worldwide distributed computing network of tens of thousands of PCs and algorithms designed to efficiently utilize this new many‐processor, highly heterogeneous, loosely coupled distributed computing paradigm, we have been able to simulate hundreds of microseconds of atomistic molecular dynamics. This has allowed us to directly simulate the folding mechanism and to accurately predict the folding rate of several fast‐folding proteins and polymers, including a nonbiological helix, polypeptide α‐helices, a β‐hairpin, and a three‐helix bundle protein from the villin headpiece. Our results demonstrate that one can reach the time scales needed to simulate fast folding using distributed computing, and that potential sets used to describe interatomic interactions are sufficiently accurate to reach the folded state with experimentally validated rates, at least for small proteins. © 2002 Wiley Periodicals, Inc. Biopolymers 68: 91–109, 2003
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.10219