Evidence map›Paper›PMID 42752891›Full record

ArticleProtein science : a publication of the Protein Society2026

ESpma: A method for assessing biological/non-biological interfaces using point-clouds-based structural features and protein language models.

Sarah Nozawa, Kentaro Tomii, Yoshinori Fukasawa

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In one paragraph

Article in Protein science : a publication of the Protein Society, 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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1 · What the graph read from it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Sarah NozawaCenter for Bioscience Research and Education, Utsunomiya University, Utsunomiya, Japan.
Kentaro TomiiArtificial Intelligence Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.ORCID 0000-0002-4567-4768
Yoshinori FukasawaCenter for Bioscience Research and Education, Utsunomiya University, Utsunomiya, Japan.ORCID 0000-0002-0882-4392

Funding

Japan Agency for Medical Research and Development JP26ama121028
6 · The paper itself

Abstract

Distinguishing biological protein-protein interfaces from non-biological contacts remains an important task in structural biology, particularly as protein complex structures continue to accumulate. Recent advances in protein language models (pLMs) have expanded their use across diverse protein prediction tasks, including sequence-based protein-protein interaction prediction. Such approaches often pool representations over entire sequences, whereas structure-based methods commonly rely on more complex graph- or geometry-based integration. We therefore asked how much interface-relevant information could be extracted by simply pooling pLM embeddings over structurally defined local regions. Here, we revisited biological-versus-crystal interface classification as a structurally well-defined testbed for this question. We developed a framework that compares full-sequence pooling, interface-localized pooling of pLM embeddings, and multimodal integration of sequence-derived embeddings with point-cloud representations of protein surfaces. On two benchmark datasets, interface-localized pooling achieved stronger performance than full-sequence or non-interacting surface pooling across three pLM backbones. Despite its simplicity, the resulting representation performed within the range of established methods that rely on explicit evolutionary analysis or geometric modeling. Incorporating explicit geometric surface information changed performance slightly, without reaching statistical significance. Because the model is linear, the interface-level score decomposes exactly into per-residue contributions, which varied within amino-acid types. Together, our results indicate that the principal gain arises from localizing pLM embeddings to physically interacting residues, enabling a lightweight and accessible implementation for biological-versus-crystal interface classification. Code and scripts are available on GitHub: https://github.com/fukasawa-group/espma.

Indexed as

Computational BiologyProtein Interaction MappingProteinsSoftwareDatabases, ProteinLarge Language ModelsModels, MolecularProtein ConformationProteinsdeep learninginterfacespoint cloudprotein complexesprotein language model

Identifiers

PMID42752891
PMCPMC13584886

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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.