Cited by 3Protein Structure and DynamicsAdvanced Physical and Chemical Molecular InteractionsComputational Drug Discovery Methods

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Data-driven enhanced sampling of mechanistic pathways

Open access
Elangovan, Revanth, Chatterjee, Sompriya, Ray, Dhiman·2025·Proceedings of the National Academy of Sciences

Published version of a preprint

Abstract

The mechanisms of molecular processes can be characterized by following the minimum free energy pathway (MFEP) on the underlying multidimensional conformational landscapes. Despite recent advancements in enhanced sampling algorithms, obtaining a converged high-dimensional molecular free energy landscape remains a considerable challenge. To circumvent this issue, we employ a deep multitask learning algorithm that integrates deep neural networks with the established enhanced sampling method of well-tempered metadynamics to iteratively learn the MFEP between reactant and product conformations, without the knowledge of the underlying free energy landscape. Our approach improves upon existing pathway exploration algorithms by following a simpler protocol, thereby eliminating the need to identify intermediate structures along a guess path. From the learned pathway, an automatic reconstruction of a mechanistic fingerprint can be performed by following the sequence of events in the molecular process, allowing for a direct characterization of the molecular mechanism. We demonstrate applications of our algorithm to prototypical chemical reactions, protein folding, and ligand–receptor binding problems. Due to its low computational cost and overall simplicity, this framework is expected to find widespread applications in elucidating molecular mechanisms at all-atom resolution.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1073/pnas.2517169122

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 72

  1. 10.1039/C7SC02664A · DOI · Paper page
  2. 10.1021/jacs.0c09105 · DOI
  3. Y. T. Pang K. M. Kuo L. Yang J. C. Gumbart Deeppath: Overcoming data scarcity for protein transition pathway prediction using physics-based deep learning. bioRxiv [Preprint] (2025). 10.1101/2025.02.27.640693 (Accessed 26 May 2025). · DOI
  4. M. Petersen R. Covino PINN-MEP: Continuous neural representations for minimum-energy path discovery in molecular systems. arXiv [Preprint] (2025). http://arxiv.org/abs/2504.16381 (Accessed 1 June 2025). · arXiv
  5. 10.1038/s43588-023-00428-z · DOI
  6. 10.33011/livecoms.4.1.1583 · DOI
  7. 10.1063/1.2719697 · DOI
  8. 10.1093/bioinformatics/btv453 · DOI
  9. 10.1063/1.1948367 · DOI
  10. 10.1002/jcc.27504 · DOI
  11. 10.1073/pnas.202427399 · DOI · Paper page
  12. 10.1016/0021-9991(77)90121-8 · DOI · Paper page
  13. 10.1016/S0009-2614(99)01123-9 · DOI
  14. 10.1021/jp0455430 · DOI
  15. 10.1063/1.2212942 · DOI
  16. 10.1016/j.cplett.2007.08.017 · DOI
  17. 10.1021/ct400469w · DOI
  18. 10.1063/1.4799236 · DOI
  19. 10.1021/acs.jctc.3c01401 · DOI
  20. 10.1016/j.bpj.2009.06.016 · DOI
  21. 10.1063/1.3544209 · DOI
  22. 10.1073/pnas.1617567114 · DOI
  23. 10.1021/acs.jctc.1c01049 · DOI
  24. 10.1021/acs.jpclett.0c00535 · DOI
  25. 10.1073/pnas.2113533118 · DOI
  26. 10.1063/1.1323224 · DOI
  27. 10.1063/1.1329672 · DOI
  28. 10.1063/1.1636455 · DOI
  29. 10.1021/acs.jcim.4c02351 · DOI
  30. 10.1021/acs.jctc.4c01032 · DOI
  31. 10.1021/acs.jpca.9b08239 · DOI
  32. 10.1063/1.1571817 · DOI
  33. 10.1063/1.474863 · DOI
  34. 10.1021/ct900689m · DOI
  35. 10.1063/1.3243080 · DOI
  36. 10.1063/1.2432340 · DOI
  37. 10.1103/PhysRevLett.109.020601 · DOI
  38. 10.1039/D2SM00888B · DOI
  39. 10.1103/PhysRevLett.123.245701 · DOI
  40. 10.1063/5.0202156 · DOI
  41. 10.1063/5.0226721 · DOI
  42. 10.1021/acs.jctc.4c00123 · DOI
  43. 10.1002/jcc.21312 · DOI
  44. 10.1063/1.4736317 · DOI
  45. 10.1021/ci00057a005 · DOI · Paper page
  46. 10.1073/pnas.2313542121 · DOI
  47. 10.1021/acs.jctc.1c01163 · DOI
  48. 10.1021/acs.jcim.4c01656 · DOI
  49. 10.1021/acs.jctc.1c00143 · DOI
  50. 10.1103/PhysRevLett.100.020603 · DOI · Paper page
  51. 10.1214/ss/1177011077 · DOI
  52. 10.1063/5.0156343 · DOI
  53. 10.1021/acs.jpclett.1c02317 · DOI
  54. 10.1016/j.cplett.2008.09.012 · DOI
  55. 10.1063/5.0258483 · DOI
  56. 10.1007/s00454-002-2886-1 · DOI
  57. 10.1021/acs.jctc.6b00212 · DOI
  58. 10.1109/TPAMI.1984.4767596 · DOI · Paper page
  59. 10.1287/moor.13.2.311 · DOI
  60. 10.1007/978-94-015-7744-1_2 · DOI
  61. 10.1021/acs.jpclett.0c01125 · DOI
  62. M. A. Pravin S. K. Singh “Enhanced sampling and free energy methods to study protein folding and dynamics” in Protein Folding Dynamics and Stability: Experimental and Computational Methods P. Saudagar T. Tripathi Eds. (Springer 2023) pp. 165–179. · DOI
  63. 10.1063/5.0239303 · DOI
  64. 10.1126/science.1208351 · DOI · Paper page
  65. 10.1021/acs.jctc.2c00806 · DOI
  66. 10.1038/s43588-025-00799-5 · DOI
  67. 10.1021/acs.jctc.1c00945 · DOI
  68. 10.1038/s41467-020-20310-0 · DOI
  69. 10.1021/acs.jctc.1c01075 · DOI
  70. 10.1080/08927022.2015.1132317 · DOI
  71. 10.1016/j.cpc.2013.09.018 · DOI
  72. 10.1063/5.0007045 · DOI · Paper page

Metadata

Authors
Elangovan, R., Chatterjee, S., & Ray, D.
Affiliations
University of Oregon (US)
Corresponding author
Ray, Dhiman
Venue
Proceedings of the National Academy of Sciences
Published
2025-12-04
Volume
122
Issue
49
Pages
e2517169122-e2517169122
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W4417002169
Cited by
3
References
1
Citations by year
2026: 2 · 2025: 1
FWCI
0.90
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
  • ChemRxiv (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
Funders
University of Oregon
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Advanced Physical and Chemical Molecular Interactions
  • Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
Keywords
enhanced sampling, well-tempered metadynamics, free energy landscape, protein folding, ligand-receptor binding, conformational landscape

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review