title: A computer simulation study of water drying at the interface of protein chains.
abstract: This study investigated the water drying (cavitation) in the interfacial region of two chains of a dimeric protein by nanosecond molecular dynamics simulations using explicit water representation. Separation-induced cavity of water was directly observed in the region. We evaluated the separation length scale of two chains on which the drying transition occurs, and the average number of water molecules that are expelled from the interfacial region during the transition. The obtained values can be rationalized by Kelvin equation for finite lateral size of confinement [K. Lum and A. Luzar, Phys. Rev. E 56, R6283 (1997)]. Also, we found that the drying transition is accompanied by an exponential reduction in the average hydrogen-bond number per interfacial water molecule. The results of this study may deepen the understanding of how hydrophobic interaction drives the assembly of protein chains.
authors.affiliation: Department of Chemistry, National Sun Yat-sen University, Kaohsiung 80424, Taiwan, Republic of China.
authors.forename: Qiang
authors.initials: Q
authors.lastname: Huang
authors.forename: Shangwu
authors.initials: S
authors.lastname: Ding
authors.forename: Chih-Yu
authors.initials: CY
authors.lastname: Hua
authors.forename: Hsiao-Ching
authors.initials: HC
authors.lastname: Yang
authors.forename: Cheng-Lung
authors.initials: CL
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D003890:Desiccation; D019281:Dimerization; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D014867:Water