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Computation of electrostatic complements to proteins: A case of charge stabilized binding
Author(s) -
Chong Lillian T.,
Dempster Sara E.,
Hendsch Zachary S.,
Lee LeePeng,
Tidor Bruce
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070122
Subject(s) - barnase , electrostatics , ligand (biochemistry) , static electricity , charge (physics) , chemistry , chemical physics , binding site , computation , electrostatic interaction , computational chemistry , biophysics , physics , computer science , biology , algorithm , quantum mechanics , biochemistry , ribonuclease , rna , receptor , gene
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.