Ligand binding hydrophobic interactions

In addition to the interactions discussed above, which all depend in part on the ioniz-ability, or at least polarizability, of the surface and the adsorbates, hydrophobic parts of ligands may bind to corresponding parts of surfaces. Thus, if a metal ion is complexed or irreversibly bonded to a hydrophobic molecule, the metal may be incorporated into the bulk or surface of a particle via hydrophobic interaction between the molecule and the solid phase. Such interactions may be quantitatively significant in systems with high concentrations of dissolved and particulate organic matter. 

FIGURE 1.4 Ligand-binding plots showing hydrogen-bonding interactions and distances and hydrophobic contacts for (a) the sucrose molecule in the A. maxima OCP structure and (b) the 3 -hydroxyechinenone molecule. Residues labeled in bold are absolutely conserved in the primary structure of the OCP. (From Wallace, A.C. et al., Protein Eng., 8, 127, 1995.)... 

Figure 10.7 The EGF receptor. The N-terminal, extracellular region of the receptor contains 622 amino acids. It displays two cysteine-rich regions, between which the ligand-binding domain is located. A 23 amino acid hydrophobic domain spans the plasma membrane. The receptor cytoplasmic region contains some 542 amino acids. It displays a tyrosine kinase domain, which includes several tyrosine autophosphorylation sites, and an actin-binding domain that may facilitate interaction with the cell cytoskeleton...

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