Evidence map›Paper›PMID 28064081›Full record

ArticleJournal of molecular graphics & modelling2017

Accuracy comparison of several common implicit solvent models and their implementations in the context of protein-ligand binding.

E V Katkova, A V Onufriev, B Aguilar, V B Sulimov

Abstract readComparative Study
In one paragraph

Article in Journal of molecular graphics & modelling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  4. Prediction of enzyme inhibition (ICJournal of molecular modeling · 2025
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  7. PocketOptimizer 2.0: A modular framework for computer-aided ligand-binding design.Protein science : a publication of the Protein Society · 2023
    Article
  8. Article
  9. Computational Design of PDZ-Peptide Binding.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Article
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  12. Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

E V KatkovaDimonta, Ltd., Nagornaya Street 15, Bldg 8, Moscow, 117186, Russia; Research Computer Center, Lomonosov Moscow State University, Leninskie Gory 1,Bldg 4, Moscow, 119992, Russia. Electronic address: katkova@dimonta.com.
A V OnufrievDepartments of Computer Science and Physics, Center for Soft Matter and Biological Physics, Virginia Tech, Blacksburg, VA, USA.
B AguilarInstitute for Systems Biology, Seattle, WA, USA.
V B SulimovDimonta, Ltd., Nagornaya Street 15, Bldg 8, Moscow, 117186, Russia; Research Computer Center, Lomonosov Moscow State University, Leninskie Gory 1,Bldg 4, Moscow, 119992, Russia.
Institute for Systems Biology · USVirginia Tech · US

Funding

Analytical Electrostatics: Methods and Biological Applications.R01GM076121 · NIGMS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI ONUFRIEV, ALEXEY VLAD · 2006 to 2014
$2.6M
DNA - DNA interactions with atomic detailR01GM099450 · NIGMS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI BAKER, NATHAN A., ONUFRIEV, ALEXEY VLAD · 2012 to 2015
$1.3M
NIGMS NIH HHS R01 GM076121NIGMS NIH HHS R01 GM099450
6 · The paper itself

Abstract

In this study several commonly used implicit solvent models are compared with respect to their accuracy of estimating solvation energies of small molecules and proteins, as well as desolvation penalty in protein-ligand binding. The test set consists of 19 small proteins, 104 small molecules, and 15 protein-ligand complexes. We compared predicted hydration energies of small molecules with their experimental values; the results of the solvation and desolvation energy calculations for small molecules, proteins and protein-ligand complexes in water were also compared with Thermodynamic Integration calculations based on TIP3P water model and Amber12 force field. The following implicit solvent (water) models considered here are: PCM (Polarized Continuum Model implemented in DISOLV and MCBHSOLV programs), GB (Generalized Born method implemented in DISOLV program, S-GB, and GBNSR6 stand-alone version), COSMO (COnductor-like Screening Model implemented in the DISOLV program and the MOPAC package) and the Poisson-Boltzmann model (implemented in the APBS program). Different parameterizations of the molecules were examined: we compared MMFF94 force field, Amber12 force field and the quantum-chemical semi-empirical PM7 method implemented in the MOPAC package. For small molecules, all of the implicit solvent models tested here yield high correlation coefficients (0.87-0.93) between the calculated solvation energies and the experimental values of hydration energies. For small molecules high correlation (0.82-0.97) with the explicit solvent energies is seen as well. On the other hand, estimated protein solvation energies and protein-ligand binding desolvation energies show substantial discrepancy (up to 10kcal/mol) with the explicit solvent reference. The correlation of polar protein solvation energies and protein-ligand desolvation energies with the corresponding explicit solvent results is 0.65-0.99 and 0.76-0.96 respectively, though this difference in correlations is caused more by different parameterization and less by methods and indicates the need for further improvement of implicit solvent models parameterization. Within the same parameterization, various implicit methods give practically the same correlation with results obtained in explicit solvent model for ligands and proteins: e.g. correlation values of polar ligand solvation energies and the corresponding energies in the frame of explicit solvent were 0.953-0.966 for the APBS program, the GBNSR6 program and all models used in the DISOLV program. The DISOLV program proved to be on a par with the other used programs in the case of proteins and ligands solvation energy calculation. However, the solution of the Poisson-Boltzmann equation (APBS program) and Generalized Born method (implemented in the GBNSR6 program) proved to be the most accurate in calculating the desolvation energies of complexes.

Indexed as

Models, MolecularLigandsProtein BindingProteinsSolventsThermodynamicsLigandsProteinsSolventsExplicit waterImplicit solvent modelsProtein-ligand bindingSolvation

Identifiers

PMID28064081
PMCPMC5313374
OpenAlexW2564199680

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.