Hydrophobicity of protein surfaces: Separating geometry from chemistry.

Abstract excerpt

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...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Bees
• Share to Dimerization
• Share to Hydrophobic and Hydrophilic Interactions