Magnitude and spatial orientation of the hydrophobic moments of multi-domain proteins

Abstract

The distributions of residue hydrophobicity for individual domains as well as for the aggregates of domains on a single chain have been found to exhibit well-defined second-order hydrophobic moment profiles. This indicates that most of the domains do fold into a stable entity with a core composed predominantly of hydrophobic residues as well as a prevalence of hydrophobic residues at the interface between domains. A simple scoring function based upon the relative hydrophobic moment dipole orientations shows that 80% of the dipoles of adjacent domains point to each other, highlighting hydrophobic residue prevalence at the domain interfaces. Copyright © 2006 Inderscience Enterprises Ltd.