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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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Published in: | Journal of chemical theory and computation 2017-11, Vol.13 (11), p.5173-5178 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 1549-9618 1549-9626 |
DOI: | 10.1021/acs.jctc.7b00791 |