Optimized Folding Simulations of Protein A

2026-07-072026-07-07http://salesiana.dossiersoluciones.com/handle/123456789/160163We 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 figuresStatistical MechanicsOptimized Folding Simulations of Protein Atext