title: Molecular dynamics characterization of protein crystal contacts in aqueous solutions.
abstract: We employ nonequilibrium molecular dynamics simulation to characterize the effective interactions between lysozyme molecules involved in the formation of two hydrophobic crystal contacts. We show that the effective interactions between crystal contacts do not exceed a few kT, the range of the attractive part of the potential is less than 4 angstroms, and, within this range, there is a significant depletion of water density between two protein contacts. Our findings highlight the different natures of protein crystallization and protein recognition processes.
authors.affiliation: Dipartimento di Fisica, Università degli Studi di Messina, Contrada Papardo, 98166 Messina, Italy.
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Pellicane
authors.forename: Graham
authors.initials: G
authors.lastname: Smith
authors.forename: Lev
authors.initials: L
authors.lastname: Sarkisov
mesh_terms: D055598:Chemical Phenomena; D003198:Computer Simulation; D003460:Crystallization; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry*; D012996:Solutions; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D012996:Solutions; D014867:Water; D009113:Muramidase