@article {bioinflmu-295,
	title = {{Evaluation of a fast implicit solvent model for molecular dynamics simulations}},
	journal = {Proteins: Structure, Function, and Bioinformatics},
	volume = {46},
	number = {1},
	year = {2002},
	pages = {24-33},
	abstract = {A solvation term based on the solvent accessible surface area (SASA)
is combined with the CHARMM polar hydrogen force field for the efficient
simulation of peptides and small proteins in aqueous solution. Only two atomic
solvation parameters are used: one is negative for favoring the direct solvation
of polar groups and the other positive for taking into account the hydrophobic
effect on apolar groups. To approximate the water screening effects on the
intrasolute electrostatic interactions, a distance-dependent dielectric function
is used and ionic side chains are neutralized. The use of an analytical
approximation of the SASA renders the model extremely efficient (i.e., only about
50\% slower than in vacuo simulations). The limitations and range of applicability
of the SASA model are assessed by simulations of proteins and structured
peptides. For the latter, the present study and results reported elsewhere show
that with the SASA model it is possible to sample a significant amount of
folding/unfolding transitions, which permit the study of the thermodynamics and
kinetics of folding at an atomic level of detail.},
	keywords = {cheminfo},
	doi = {10.1002/prot.10001},
	author = {Philippe Ferrara and Joannis Apostolakis and Amedeo Caflisch}
}