New Coarse Variables for the Accurate Determination of Standard Binding Free Energies

To improve sampling of the configurational entropy change upon protein–ligand binding, we have introduced a new set of coarse variables describing the relative orientation and position of the ligand via a global macromolecular orientational procedure, onto which geometrical restraints are applied. E...

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Bibliographic Details
Published in:Journal of chemical theory and computation 2017-11, Vol.13 (11), p.5173-5178
Main Authors: Fu, Haohao, Cai, Wensheng, Hénin, Jérôme, Roux, Benoît, Chipot, Christophe
Format: Article
Language:English
Subjects:
Binding
Binding Sites
Chemical Sciences
Entropy
Free energy
Ligands
Models, Molecular
or physical chemistry
Protein Binding
Proteins
src Homology Domains
Theoretical and
Thermodynamics
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Summary:To improve sampling of the configurational entropy change upon protein–ligand binding, we have introduced a new set of coarse variables describing the relative orientation and position of the ligand via a global macromolecular orientational procedure, onto which geometrical restraints are applied. Evaluating the potential of mean force for the different coarse variables, the experimental standard binding free energy for three decapeptides associated with the SH3 domain of the Abl kinase is reproduced quantitatively.
ISSN:1549-9618
1549-9626
DOI:10.1021/acs.jctc.7b00791