Abstract
This paper uses a recently developed computer model to study the energetics of solvent-exposed salt-bridges. The model uses the “mining minima” method to compute conformational free energies with the CHARMm empirical force and the generalized Born solvation model. Satisfactory agreement is obtained in comparison with the measured binding affinities of ion pairs in solution and with the salt-bridge energetics deduced from studies of salt-bridges in helical peptides. The calculations suggest that stabilizing charge−charge interactions in helical peptides do not require well-defined salt-bridge conformations. This is in agreement with crystallographic studies of charge pairs added to T4 lysozyme by site-directed mutagenesis. The computer model is also used to make a testable prediction that arginine and phosphotyrosine residues in an (i, i + 4) relationship will form a particularly strong salt-bridge in helical peptides. The biological implications of these results are discussed.
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