Evidence map›Paper›PMID 31185169›Full record

ArticleJournal of chemical theory and computation2019

Robust Free Energy Perturbation Protocols for Creating Molecules in Solution.

Israel Cabeza de Vaca, Ricardo Zarzuela, Julian Tirado-Rives, William L Jorgensen

Abstract read
In one paragraph

Article in Journal of chemical theory and computation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Enthalpies and entropies of hydration from Monte Carlo simulations.Physical chemistry chemical physics : PCCP · 2024
    Article
  5. How Robust Is the Ligand Binding Transition State?Journal of the American Chemical Society · 2023
    Article
  6. Recent PELE Developments and Applications in Drug Discovery Campaigns.International journal of molecular sciences · 2022
    Review
  7. Computational Tools for Accurate Binding Free-Energy Prediction.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Article
  9. Article
  10. 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.

Israel Cabeza de VacaDepartment of Chemistry , Yale University , New Haven , Connecticut 06520-8107 , United States.
Ricardo ZarzuelaDepartment of Physics and Astronomy , University of California , Los Angeles , California 90095 , United States.
Julian Tirado-RivesDepartment of Chemistry , Yale University , New Haven , Connecticut 06520-8107 , United States.ORCID http://orcid.org/0000-0001-7330-189X
William L JorgensenDepartment of Chemistry , Yale University , New Haven , Connecticut 06520-8107 , United States.ORCID http://orcid.org/0000-0002-3993-9520

Funding

POTENTIAL FUNCTIONS FOR WATER PROTEIN INTERACTIONSR01GM032136 · NIGMS · YALE UNIVERSITY · PI JORGENSEN, WILLIAM L. · 1985 to 2023
$8.2M
NIGMS NIH HHS R01 GM032136
6 · The paper itself

Abstract

Accurate methods to estimate free energies play an important role for studying diverse condensed-phase problems in chemistry and biochemistry. The most common methods used in conjunction with molecular dynamics (MD) and Monte Carlo statistical mechanics (MC) simulations are free energy perturbation (FEP) and thermodynamic integration (TI). For common applications featuring the conversion of one molecule to another, simulations are run in stages or multiple "λ-windows" to promote convergence of the results. For computation of absolute free energies of solvation or binding, calculations are needed in which the solute is typically annihilated in the solvent and in the complex. The present work addresses identification of optimal protocols for such calculations, specifically, the creation/annihilation of organic molecules in aqueous solution. As is common practice, decoupling of the perturbations for electrostatic and Lennard-Jones interactions was performed. Consistent with earlier reports, FEP calculations for molecular creations are much more efficient, while annihilations require many more windows and may converge to incorrect values. Strikingly, we find that as few as four windows may be adequate for creation calculations for solutes ranging from argon to ethylbenzene. For a larger druglike molecule, MIF180, which contains 22 non-hydrogen atoms and three rotatable bonds, 10 creation windows are found to be adequate to yield the correct free energy of hydration. Convergence is impeded with procedures that use any sampling in the annihilation direction, and there is no need for postprocessing methods such as the Bennett acceptance ratio (BAR).

Identifiers

PMID31185169
PMCPMC6615964

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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.