Macromolecular recognition electrostatics

An understanding of a wide variety of phenomena concerning conformational stabilities and molecule-molecule association (protein-protein, protein-ligand, and protein-nucleic acid) requires consideration of solvation effects. In particular, a quantitative assessment of the relative contribution of hydrophobic and electrostatic interactions in macromolecular recognition is a problem of central importance in biology. 

Matthew JB. Electrostatic and dynamic aspects of macromolecular recognition. In Beveridge DL, Lavery R, eds. Theoretical Biochemistry Molecular Biophysics. Vol. 2 Proteins. Schenectady, NY Adenine, 1991 107-120. 

The interaction between a solvated peptide or protein and a chemically modified RPC and HIC stationary phase in a fully or partially aqueous solvent environment can be discussed in terms of the interplay of weak physical forces. The main types of physical interactions that are involved in order of relevance and dominance for the establishment of the selective recognition and binding between a peptide or protein and RPC and HIC ligates are (I) hydrophobic interactions and related phenomena mediated by polarized electron donor or electron acceptor processes, (2) Lifshitz-London forces and van der Waals and associated weak dipolar interactions, (3) tt 7t and n ->dipole interactions, (4) hydrogen bond interactions, (5) electrostatic interactions, (6) metal ion coordination interactions, and (7) secondary macromolecular interactions involving force field effects. 

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