High-resolution protein folding with a transferable potential
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Date
2005
Author(s)
Hubner, Isaac A.
Deeds, Eric J.
Shakhnovich, Eugene I.
Publisher
National Academy of Sciences
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Citation
Hubner, I. A., E. J. Deeds, and E. I. Shakhnovich. 2005. “High-Resolution Protein Folding with a Transferable Potential.” Proceedings of the National Academy of Sciences102 (52): 18914–19. https://doi.org/10.1073/pnas.0502181102.
Abstract
A generalized computational method for folding proteins with a fully transferable potential and geometrically realistic all-atom model is presented and tested on seven helix bundle proteins. The protocol, which includes graph-theoretical analysis of the ensemble of resulting folded conformations, was systematically applied and consistently produced structure predictions of approximate to 3 angstrom without any knowledge of the native state. To measure and understand the significance of the results, extensive control simulations were conducted. Graph theoretic analysis provides a means for systematically identifying the native fold and provides physical insight, conceptually linking the results to modern theoretical views of protein folding. In addition to presenting a method for prediction of structure and folding mechanism, our model suggests that an accurate all-atom amino acid representation coupled with a physically reasonable atomic interaction potential and hydrogen bonding are essential features for a realistic protein model.
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