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Contribution of Ligand Desolvation to Binding Thermodynamics in a Ligand–Protein Interaction
Author(s) -
Shimokhitalia,
Bronowska Agnieszka,
Homans Steve W.
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200602227
Subject(s) - solvation , chemistry , ligand (biochemistry) , affinities , implicit solvation , molecular dynamics , thermodynamics , protein ligand , computational chemistry , solvent , chemical physics , stereochemistry , biochemistry , physics , receptor
Solvation is free : The affinities within biomolecular associates are governed by a complex interplay between structure and dynamics of the interacting species and solvent water. The contribution of ligand desolvation in the binding of small ligands to the major urinary protein has been examined to give a complete breakdown of binding thermodynamics in this system.