Jeffrey K. Weber, Seung-Gu Kang, et al.
Biophysical Journal
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.
Jeffrey K. Weber, Seung-Gu Kang, et al.
Biophysical Journal
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Aging
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Journal of Physiology
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ICLR 2025