Hydrophobicity of protein surfaces: Separating geometry from chemistry.

ABSTRACT: To better understand the role of surface chemical heterogeneity in natural nanoscale hydration, we study via molecular dynamics simulation the structure and thermodynamics of water confined between two protein-like surfaces. Each surface is constructed to have interactions with water corresponding to those of the putative hydrophobic surface of a melittin dimer, but is flattened rather than having its native "cupped" configuration. Furthermore, peripheral charged groups are removed. Thus, the role of a rough surface topography is removed, and results can be productively compared with those previously observed for idealized, atomically smooth hydrophilic and hydrophobic flat surfaces. The results indicate that the protein surface is less hydrophobic than the idealized counterpart. The densi

SUBMITTER: Giovambattista N 

PROVIDER: S-EPMC2268126 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature