Paper Citing NAMD - Abstract
Saito, Hiroaki; Matubayasi, Nobuyuki; Nishikawa, Kiyoshi; Nagao, Hidemi
Hydration property of globular proteins: An analysis of solvation free energy by energy representation method
CHEMICAL PHYSICS LETTERS, 497:218-222, SEP 20 2010
Molecular dynamics simulations and solvation free energy calculations of five globular proteins (BPTI, RNase A, Lysozyme, beta-lactoglobulin A, and alpha-chymotrypsinogen A) have been carried out to elucidate the hydration properties. Solvation free energies of the proteins with explicit solvent were estimated by energy representation (ER) method. The calculated solvation free energies were correlated with the solvent accessible surface area of hydrophilic portion, being consistent with the hydrophilic property of the proteins. These results showed that the ER method should be a powerful tool for estimating the hydration property of proteins, showing a progress of the free energy calculation with explicit solvent. (c) 2010 Elsevier B.V. All rights reserved.
