Evidence map›Paper›PMID 40058108›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2025

Leveraging AlphaFold2 and residual dipolar couplings for side-chain methyl group assignment: A case study with S. cerevisiae Xrs2.

Ajeak Vigneswaran, Tanner A Buschmann, Michael P Latham

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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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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

2 citing papers in PubMed.

  1. Article
  2. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2025
    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

3 authors.

Ajeak VigneswaranDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, United States.
Tanner A BuschmannDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX, United States.
Michael P LathamDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, United States. Electronic address: latha070@umn.edu.

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Structural Biology Studies of a Large DNA Repair ComplexR35GM128906 · NIGMS · UNIVERSITY OF MINNESOTA · PI Michael Parker Latham · 2018 to 2026
$3.1M
NCI NIH HHS P30 CA046934NIGMS NIH HHS R35 GM128906
6 · The paper itself

Abstract

Side-chain methyl group NMR spectroscopy provides invaluable insights into macromolecular structure, dynamics, and function, particularly for large biomolecular complexes. Accurate assignment of methyl group resonances in two-dimensional spectra is essential for structural and dynamics studies. Traditional methyl group assignment strategies rely on either transferring assignments from backbone resonance data or NOESY data and high-resolution experimental structures; however, these methods are often limited by molecular size or availability of structural information, respectively. Here, we describe the use of AlphaFold2 structural models as a basis for the manual, distance-based assignment of side-chain methyl group resonances in the folded domains of S. cerevisiae Xrs2. While AlphaFold2 models facilitated initial assignments for the methyl resonances, inaccuracies in the side-chain coordinates highlighted the need for improved structural models. By generating >500 ColabFold-derived models and filtering with methyl residual dipolar couplings (RDCs), we identified structural models with superior agreement to experimental data. These refined models enabled additional methyl group assignments while suggesting an iterative approach to simultaneously improve structure prediction and resonance assignment. Our findings outline a workflow that integrates machine learning-based structural predictions with experimental NMR data, offering a pathway for advancing methyl group assignment in systems lacking high-resolution experimental structures.

Indexed as

Nuclear Magnetic Resonance, BiomolecularSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAlgorithmsMagnetic Resonance SpectroscopyMethylationModels, MolecularSaccharomyces cerevisiae ProteinsAlphaFold2Methyl-based NMRResidual dipolar couplingsResonance assignments

Identifiers

PMID40058108
PMCPMC11993329

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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.