Magnitude and spatial orientation of the hydrophobic moments of multi-domain proteins
by Ruhong Zhou, Ajay Royyuru, Prasanna Athma, Frank Suits, B. David Silverman
International Journal of Bioinformatics Research and Applications (IJBRA), Vol. 2, No. 2, 2006

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.

Online publication date: Tue, 09-May-2006

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