Volume 67, Number 2, July 2004
|307 - 313
|Interdisciplinary physics and related areas of science and technology
|01 July 2004
All-atom folding of the trp-cage protein with an adpative parallel tempering method
Forschungszentrum Karlsruhe, Institut für Nanotechnologie P.O. Box 3640, 76021 Karlsruhe, Germany
Accepted: 5 May 2004
Using the recently developed protein free-energy force field PFF01 we report the reproducible all-atom folding of the 20 amino acid trp-cage protein to within 2.0 backbone RMS deviation to the experimental structure with modest computational resources. We used an adapted version of the parallel tempering method as an inherently parallel stochastic optimization method. We find that near native structures dominate the low-energy spectrum of the final conformations and investigate the efficiency of the method as a function of the number of replicas in application to all-atom protein structure prediction.
PACS: 87.15.-v – Biomolecules: structure and physical properties / 87.15.Aa – Theory and modeling; computer simulation / 02.60.Pn – Numerical optimization
© EDP Sciences, 2004
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