DOI | Resolve DOI: https://doi.org/10.1007/978-1-61779-465-0_19 |
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Author | Search for: Sulea, Traian1; Search for: Purisima, Enrico O.1 |
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Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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Format | Text, Article |
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Subject | binding free energy; scoring function; protein-ligand binding; molecular dynamics |
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Abstract | The solvated interaction energy (SIE) is an end-point, physics-based scoring function for predicting ligand-binding affinities. It supplements the force-field interaction energy with the desolvation cost of binding. Parameters such as the solute dielectric constant, Born radii, a cavity term and an overall scaling coefficient and additive constant have been previously calibrated against a training set of 99 protein–ligand complexes. We describe the application of the method to estimating binding free energies from molecular dynamics trajectories of protein–ligand binding complexes. |
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Publication date | 2012 |
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In | |
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Series | |
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Language | English |
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Peer reviewed | Yes |
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NRC number | NRCC 53202 |
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NPARC number | 21268278 |
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Export citation | Export as RIS |
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Report a correction | Report a correction (opens in a new tab) |
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Record identifier | a9f3d349-72f5-4a79-845e-0967dd29c44b |
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Record created | 2013-06-13 |
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Record modified | 2020-04-21 |
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