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Fig. 6.17 The 1DVZ protein: 3D representation ( top ) with ligand binding residues marked in
yellow and complexation interface marked in pink . The cyan-colored fragment (69-80) corre-
sponds to the greatest divergence between the observed (O) and theoretical (T) distribution of
hydrophobicity in the
Δ H pro fi le ( bottom )
The summary of structural analysis of the proteins discussed in Table 6.2 are
given in Table 6.3 .
No particular correlation can be found for characteristics of protein-protein com-
plexes as shown in Table 6.3 . The HADDOCK program was the best for complex-
ation interface characterized by the lowest number of hydrophobic residues engaged
in complexation.
The “fuzzy oil drop” model identifies complexation sites as specific deforma-
tions in the protein's hydrophobic core associated with the presence of residues
whose actual hydrophobicity values diverge from theoretical predictions. When the
core is perturbed by more than one external molecule (for instance by a protein and
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