Evidence map›Paper›PMID 41880461›Full record

ArticlePLoS computational biology2026

Overcoming extrapolation challenges of deep learning by incorporating physics in protein sequence-function modeling.

Shrishti Barethiya, Jian Huang, Clarice Stumpf, Xiao Liu, Hui Guan, Jianhan Chen

Abstract read
In one paragraph

Article in PLoS computational biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Shrishti BarethiyaDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, United States of America.
Jian HuangDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, United States of America.
Clarice StumpfDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, United States of America.
Xiao LiuCollege of Information and Computer Sciences, University of Massachusetts, Amherst, Massachusetts, United States of America.
Hui GuanCollege of Information and Computer Sciences, University of Massachusetts, Amherst, Massachusetts, United States of America.
Jianhan ChenDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, United States of America.ORCID https://orcid.org/0000-0002-5281-1150

Funding

Disordered Proteins and Dynamic Interactions in Biology and Diseases.R35GM144045 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI Jianhan Chen · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM144045
6 · The paper itself

Abstract

Understanding protein sequence-to-function relationship is crucial to assist studies of genetic diseases, protein evolution, and protein engineering. The sequence-to-function relationship of proteins is inherently complex due to multi-site high-dimensional correlation and structural dynamics. Deep learning algorithms such as (graph) convolutional neural networks and recently transformers have become very popular for learning the protein sequence-to-function mapping from deep mutational scanning data and available structures. However, it remains very challenging for these models to achieve accurate extrapolation when predicting functional effect of variants with positions or mutation types not seen in the training data. We propose that incorporating the physics of protein interactions and dynamics can be an effective approach to overcome the extrapolation limitations. Specifically, we demonstrate that biophysics-based modeling can be used to quantify the energetic effects of mutations and that incorporating these physical energetics directly within the convolution and graph convolution neural networks can significantly improve the performance of positional and mutational extrapolation compared to models without biophysics-inspired features. Our results support the effectiveness of leveraging physical knowledge in overcoming the limitation of data scarcity.

Indexed as

Deep LearningProteinsAlgorithmsAmino Acid SequenceComputational BiologyConvolutional Neural NetworksGraph Neural NetworksModels, MolecularMutationProteins

Identifiers

PMID41880461
PMCPMC13048498

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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.