Evidence map›Paper›PMID 36979392›Full record

ArticleBiomolecules2023

Protein Design Using Physics Informed Neural Networks.

Sara Ibrahim Omar, Chen Keasar, Ariel J Ben-Sasson, Eldad Haber

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Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Applications and limitations of AI tools in enzyme design.Protein science : a publication of the Protein Society · 2026
    Review
  2. Article
  3. Biomolecular Interaction Prediction: The Era of AI.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  4. Article
  5. Biophysics-based protein language models for protein engineering.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. 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.

Sara Ibrahim OmarProteic Bioscience Inc., Vancouver, BC V7T 1C0, Canada.ORCID 0000-0002-0133-3531
Chen KeasarDepartment of Computer Science, Ben Gurion University of the Negev, Be'er Sheva 84105, Israel.
Ariel J Ben-SassonIndependent Researcher, Haifa 3436301, Israel.ORCID 0000-0003-3395-6327
Eldad HaberDepartment of Earth Ocean and Atmospheric Sciences, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inverse protein folding problem, also known as protein sequence design, seeks to predict an amino acid sequence that folds into a specific structure and performs a specific function. Recent advancements in machine learning techniques have been successful in generating functional sequences, outperforming previous energy function-based methods. However, these machine learning methods are limited in their interoperability and robustness, especially when designing proteins that must function under non-ambient conditions, such as high temperature, extreme pH, or in various ionic solvents. To address this issue, we propose a new Physics-Informed Neural Networks (PINNs)-based protein sequence design approach. Our approach combines all-atom molecular dynamics simulations, a PINNs MD surrogate model, and a relaxation of binary programming to solve the protein design task while optimizing both energy and the structural stability of proteins. We demonstrate the effectiveness of our design framework in designing proteins that can function under non-ambient conditions.

Indexed as

Neural Networks, ComputerProteinsAmino Acid SequenceMolecular Dynamics SimulationPhysicsProteinsbinary optimizationphysics-informed neural networksprotein design

Identifiers

PMID36979392
PMCPMC10046838

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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.