title: Hydrogen-bond dynamics in the air-water interface.
abstract: Hydrogen-bond (H-bond) dynamics in the air-water interface is studied by molecular dynamics simulations. The analysis reveals that the dynamics of breaking and forming hydrogen bonds in the air-water interface is faster than that in bulk water for the polarizable water models. This is in contrast to the results found on a protein surface. We show that the difference stems from more rapid translational diffusion in the interface. When the effect of pair diffusion is eliminated, the hydrogen-bond dynamics in the interface is observed to be slower than that in the bulk. This occurs because the number of water molecules adjacent to a hydrogen-bonded pair and available to accept or donate a hydrogen bond is smaller in the interface than in the bulk. The comparison between polarizable water models and fixed-charge models highlights the potential importance of the polarization effect in the water-vapor interface.
authors.affiliation: Department of Chemistry and Center for Bimolecular Simulation, Columbia University, 3000 Broadway, New York, New York 10027, USA.
authors.forename: Pu
authors.initials: P
authors.lastname: Liu
authors.forename: Edward
authors.initials: E
authors.lastname: Harder
authors.forename: B J
authors.initials: BJ
authors.lastname: Berne
mesh_terms: D000388:Air; D001703:Biophysics / Q000379:methods*; D002627:Chemistry, Physical / Q000379:methods*; D003198:Computer Simulation; D004058:Diffusion; D006860:Hydrogen Bonding; D007700:Kinetics; D008956:Models, Chemical; D015233:Models, Statistical; D008968:Molecular Conformation; D011336:Probability; D011506:Proteins / Q000737:chemistry; D013499:Surface Properties; D013696:Temperature; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D014867:Water