Optimized Folding Simulations of Protein A
Statistical Mechanics
2008-05-05 v2
Abstract
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.
Keywords
Cite
@article{arxiv.0711.3830,
title = {Optimized Folding Simulations of Protein A},
author = {S. Trebst and U. H. E. Hansmann},
journal= {arXiv preprint arXiv:0711.3830},
year = {2008}
}
Comments
6 pages, 8 figures