Patch analysis distributions: rank ordering
of observed interface patches relative to
High ASA other patches on the surface of the protein. For
e each protein, the interface patch is ranked, relative
to all other surface patches, as being in the
top 10%, 10-20% etc. (see Fig. 7). The 32
observations (one for each homodimer) are combined
for each parameter separately. The distributions
shown are rms deviation of atoms from
the least-squares plane through the atoms (0-
10% are the most planar interfaces) (a), interface
residue propensities (b), protrusion index (c),
hydrophobicity [based on the scale of Janin et al.
(9)] (d), and ASA (e). A mean ASA for residues
90' 100 in each patch was calculated and used in the rank
ordering.