Dispersion terms and analysis of size- and charge dependence in an enhanced Poisson-Boltzmann approach.
We implement a well-established concept to consider dispersion effects within a Poisson-Boltzmann approach of continuum solvation of proteins. The theoretical framework is particularly suited for boundary element methods. Free parameters are determined by comparison to experimental data as well as high-level quantum mechanical reference calculations. The method is general and can be easily extended in several directions. The model is tested on various chemical substances and found to yield good-quality estimates of the solvation free energy without obvious indication of any introduced bias. Once optimized, the model is applied to a series of proteins, and factors such as protein size or partial charge assignments are studied.
Kar
Parimal
P
Department of Physics, Michigan Technological University, 1400 Townsend Drive, Houghton, Michigan 49931-1295, USA.
Seel
Max
M
Hansmann
Ulrich H E
UH
Höfinger
Siegfried
S
D000465:Algorithms; D008958:Models, Molecular; D010316:Particle Size; D016012:Poisson Distribution; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry; D013816:Thermodynamics
D011506:Proteins; D012996:Solutions