Evidence map›Paper›PMID 32696381›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions.

Kristine Steen Jensen

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. 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
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.

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

1 author.

Kristine Steen JensenDepartment for Biophysical Chemistry, Center for Molecular Protein Science, LTH, Lund University, Lund, Sweden. kristine.steen_jensen@bpc.lu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many intrinsically disordered proteins (IDPs) adopt a well-defined structure upon binding to their interaction partners. Kinetic characterization is a requirement for the investigation of the dynamics and mechanisms of these folding-upon-binding reactions. Here a protocol is described for the investigation of binding kinetics of bimolecular binding and folding reactions of IDPs to their ligand partner under pseudo-first-order conditions using stopped-flow mixing and fluorescence detection.

Indexed as

Protein BindingProtein FoldingEquipment DesignIntrinsically Disordered ProteinsKineticsLigandsModels, MolecularProtein ConformationSpectrometry, FluorescenceThermodynamicsIntrinsically Disordered ProteinsLigandsAssociation and dissociation rate constantsBinding mechanismsDisplacement kineticsFolding and bindingIDPIntrinsically disordered proteinsStopped-flow measurements

Identifiers

PMID32696381

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.