Computation of electrostatic complements to proteins: A case of charge stabilized binding
Open Access
- 1 January 1998
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 7 (1) , 206-210
- https://doi.org/10.1002/pro.5560070122
Abstract
Recent evidence suggests that the net effect of electrostatics is generally to destabilize protein binding due to large desolvation penalties. A novel method for computing ligand-charge distributions that optimize the tradeoff between ligand desolvation penalty and favorable interactions with a binding site has been applied to a model for barnase. The result is a ligand-charge distribution with a favorable electrostatic contribution to binding due, in part, to ligand point charges whose direct interaction with the binding site is unfavorable, but which make strong intra-molecular interactions that are uncloaked on binding and thus act to lessen the ligand desolvation penalty.Keywords
Funding Information
- National Institutes of Health (GM47678 and GM56552)
- MIT
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