Optimized Folding Simulations of Protein A

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We describe optimized parallel tempering simulations of the 46-residue B-fragment of protein A. Native-like configurations with a root-mean-square deviation of approximately 3A to the experimentally determined structure (Protein Data Bank identifier 1BDD) are found. However, at biologically relevant temperatures such conformations appear with only about 10% frequency in our simulations. Possible short comings in our energy function are discussed.
6 pages, 8 figures

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Statistical Mechanics

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http://salesiana.dossiersoluciones.com/handle/123456789/160163

Consulte el texto completo en el siguiente enlace:

https://arxiv.org/abs/0711.3830
 http://arxiv.org/abs/0711.3830
 Eur. Phys. J. E 24, 311 (2007).
 doi:10.1140/epje/i2007-10241-1

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arXiv