Evidence map›Paper›PMID 38317055›Full record

ArticleBioinformatics (Oxford, England)2024

PMIpred: a physics-informed web server for quantitative protein-membrane interaction prediction.

Niek van Hilten, Nino Verwei, Jeroen Methorst, Carsten Nase, Andrius Bernatavicius, Herre Jelger Risselada

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

The trial behind it

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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

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  14. The role of amphipathic and cationic helical peptides in Parkinson's disease.Protein science : a publication of the Protein Society · 2025
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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

6 authors.

Niek van HiltenLeiden Institute of Chemistry, Leiden University, Leiden 2333 CC, Netherlands.ORCID 0000-0003-1204-2489
Nino VerweiLeiden Institute of Chemistry, Leiden University, Leiden 2333 CC, Netherlands.ORCID 0000-0003-2464-6896
Jeroen MethorstLeiden Institute of Chemistry, Leiden University, Leiden 2333 CC, Netherlands.
Carsten NaseDepartment of Physics, Technical University Dortmund, Dortmund 44227, Germany.
Andrius BernataviciusLeiden Institute of Advanced Computer Science, Leiden University, Leiden 2333 CA, Netherlands.
Herre Jelger RisseladaLeiden Institute of Chemistry, Leiden University, Leiden 2333 CC, Netherlands.

Funding

Deutsche ForschungsgemeinschaftDutch Research OrganisationNWO Vidi scheme
6 · The paper itself

Abstract

motivationMany membrane peripheral proteins have evolved to transiently interact with the surface of (curved) lipid bilayers. Currently, methods to quantitatively predict sensing and binding free energies for protein sequences or structures are lacking, and such tools could greatly benefit the discovery of membrane-interacting motifs, as well as their de novo design.

resultsHere, we trained a transformer neural network model on molecular dynamics data for >50 000 peptides that is able to accurately predict the (relative) membrane-binding free energy for any given amino acid sequence. Using this information, our physics-informed model is able to classify a peptide's membrane-associative activity as either non-binding, curvature sensing, or membrane binding. Moreover, this method can be applied to detect membrane-interaction regions in a wide variety of proteins, with comparable predictive performance as state-of-the-art data-driven tools like DREAMM, PPM3, and MODA, but with a wider applicability regarding protein diversity, and the added feature to distinguish curvature sensing from general membrane binding. AVAILABILITY AND IMPLEMENTATION: We made these tools available as a web server, coined Protein-Membrane Interaction predictor (PMIpred), which can be accessed at https://pmipred.fkt.physik.tu-dortmund.de.

Indexed as

Membrane ProteinsPeptidesAmino Acid SequenceNeural Networks, ComputerPhysicsMembrane ProteinsPeptides

Identifiers

PMID38317055
PMCPMC11212490

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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.