TY  - JOUR
AU  - Tarenzi, Thomas
AU  - Calandrini, Vania
AU  - Potestio, Raffaello
AU  - Giorgetti, Alejandro
AU  - Carloni, Paolo
TI  - Open Boundary Simulations of Proteins and Their Hydration Shells by Hamiltonian Adaptive Resolution Scheme
JO  - Journal of chemical theory and computation
VL  - 13
IS  - 11
SN  - 1549-9626
CY  - Washington, DC
M1  - FZJ-2017-07069
SP  - 5647–5657
PY  - 2017
AB  - The recently proposed Hamiltonian Adaptive Resolution Scheme (H-AdResS) allows to perform molecular simulations in an open boundary framework. It allows to change on the fly the resolution of specific subset of molecules (usually the solvent), which are free to diffuse between the atomistic region and the coarse-grained reservoir. So far, the method has been successfully applied to pure liquids. Coupling the H-AdResS methodology to hybrid models of proteins, such as the Molecular Mechanics/Coarse-Grained (MM/CG) scheme, is a promising approach for rigorous calculations of ligand binding free energies in low-resolution protein models. Towards this goal, here we apply for the first time H-AdResS to two atomistic proteins in dual-resolution solvent, proving its ability to reproduce structural and dynamic properties of both the proteins and the solvent, as obtained from atomistic simulations.
LB  - PUB:(DE-HGF)16
C6  - pmid:28992702
UR  - <Go to ISI:>//WOS:000415911800041
DO  - DOI:10.1021/acs.jctc.7b00508
UR  - https://juser.fz-juelich.de/record/838466
ER  -