Nuclear Magnetic Resonance-Guided Structural Analysis of Moderate-Affinity Protein Complexes with Intrinsically Disordered Polypeptides.

Dmitri Tolkatchev, Garry E Smith, Alla S Kostyukova

Open access · greenAbstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact, top 89% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 at 1 institution in 1 country.

Dmitri TolkatchevVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA. dmitri.tolkatchev@wsu.edu.

Garry E SmithVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA.

Alla S KostyukovaVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA.

Washington State University · US

Funding

REGULATION OF THE ACTIN FILAMENT POINTED END DYNAMICS IN HEALTH AND DISEASER01GM120137 · NIGMS · WASHINGTON STATE UNIVERSITY · PI GALKIN, VITOLD, GREGORIO, CAROL C · 2017 to 2024

$4.0M

NIGMS NIH HHS R01 GM120137

6 · The paper itself

Abstract

Binding affinity of an individual binding site of an intrinsically disordered protein for its folded partner may be moderate. In such cases, a straightforward determination of the structure of the binding interface is difficult. We offer a hybrid protocol combining NMR chemical shift information, NMR spectral data on amino acid residue sequence substitution effects, residual dipolar coupling, and molecular dynamics simulation that allowed us to determine the structure of a complex between the intrinsically disordered tropomyosin-binding site of leiomodin and a coiled-coil peptide modeling the N-terminal fragment of tropomyosin. The protocol can be used for other moderate-affinity complexes composed of an intrinsically disordered peptide bound to a structured protein partner.

Indexed as

Intrinsically Disordered ProteinsTropomyosinMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularPeptidesProtein BindingIntrinsically Disordered ProteinsPeptidesTropomyosinComplexExpression tagIntrinsically disordered proteinsLeiomodinMolecular dynamics simulationNuclear magnetic resonanceStructureTropomyosin

Identifiers

PMID37093489

DOI10.1007/978-1-0716-3147-8_23

PMCPMC11273159

OpenAlexW4366819714

What OpenQuestion holds

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Registered trials

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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.