Evidence map›Paper›PMID 35769913›Full record

ArticleFrontiers in molecular biosciences2022

AlphaFold Models of Small Proteins Rival the Accuracy of Solution NMR Structures.

Roberto Tejero, Yuanpeng Janet Huang, Theresa A Ramelot, Gaetano T Montelione

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
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  5. Modernizing biomolecular NMR: The POKY suite.The Journal of biological chemistry · 2026
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  14. Predicting multiple conformations of ligand binding sites in proteins suggests that AlphaFold2 may remember too much.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

4 authors at 2 institutions in 2 countries.

Roberto TejeroDepartamento de Química Física, Universidad de Valencia, Valencia, Spain.
Yuanpeng Janet HuangDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Sciences, Rensselaer Polytechnic Institute, Troy, NY, United States.
Theresa A RamelotDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Sciences, Rensselaer Polytechnic Institute, Troy, NY, United States.
Gaetano T MontelioneDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Sciences, Rensselaer Polytechnic Institute, Troy, NY, United States.
Rensselaer Polytechnic Institute · USUniversitat de València · ES

Funding

Hybrid Methods for Dynamic Structure Analysis of Proteins from Pathogenic MicroorganismsR35GM141818 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI MONTELIONE, GAETANO T · 2021 to 2025
$3.3M
Membrane Protein Structure Using Evolutionary Couplings and Sparse NMR DataR01GM120574 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2017 to 2020
$2.3M
NIGMS NIH HHS R35 GM141818
6 · The paper itself

Abstract

Recent advances in molecular modeling using deep learning have the potential to revolutionize the field of structural biology. In particular, AlphaFold has been observed to provide models of protein structures with accuracies rivaling medium-resolution X-ray crystal structures, and with excellent atomic coordinate matches to experimental protein NMR and cryo-electron microscopy structures. Here we assess the hypothesis that AlphaFold models of small, relatively rigid proteins have accuracies (based on comparison against experimental data) similar to experimental solution NMR structures. We selected six representative small proteins with structures determined by both NMR and X-ray crystallography, and modeled each of them using AlphaFold. Using several structure validation tools integrated under the Protein Structure Validation Software suite (PSVS), we then assessed how well these models fit to experimental NMR data, including NOESY peak lists (RPF-DP scores), comparisons between predicted rigidity and chemical shift data (ANSURR scores), and

Indexed as

AlphaFoldartificial inteligenceautomated structure determinationprotein NMRprotein structure predictionstructure validationX-ray crystal structure analysis

Identifiers

PMID35769913
PMCPMC9234698
OpenAlexW4282840217

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.