A Quick Primer in Fluorescence-Based Equilibrium and Pre-steady State Methods for Determining Protein-Nucleotide Affinities.

Harland E Brandon, Hans-Joachim Wieden

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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. 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

3.5field-weighted citation impact, top 7% 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.

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2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Harland E BrandonDepartment of Chemistry and Biochemistry, Alberta RNA Research and Training Institute (ARRTI), University of Lethbridge, Lethbridge, AB, Canada.

Hans-Joachim WiedenDepartment of Chemistry and Biochemistry, Alberta RNA Research and Training Institute (ARRTI), University of Lethbridge, Lethbridge, AB, Canada. hj.wieden@uleth.ca.

University of Lethbridge · CA

Funding

CIHR MOP246392

6 · The paper itself

Abstract

Biomolecular interactions facilitate the biochemical processes that sustain life. Proteins, RNAs, and ribonucleoprotein complexes perform cellular functions that range from catalyzing the formation or cleavage of bonds to being structural building blocks, both of which are only possible through the interaction with their respective biomolecular partner(s). Having access to the parameters that describe these interactions is important for our understanding of the principles that underlie enzymatic and nonenzymatic processes. Here we describe two fluorescence-based approaches to determine two key parameters, the affinity and the rate of association/dissociation of a protein and a ligand. Considerations are provided to expand the described approach to other experimental systems.

Indexed as

Escherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferFluorescent DyesGTP-Binding ProteinsKineticsProtein BindingRNA, BacterialEscherichia coli ProteinsFluorescent DyesGTP-Binding ProteinsHflX protein, E coliRNA, BacterialAffinityEquilibrium bindingFluorescenceFRETGTPaseNucleotidePre-steady stateStopped-flow

Identifiers

PMID33877603

DOI10.1038/s41598-019-40480-2

OpenAlexW3154926552

What OpenQuestion holds

Textmetadata

Read underepoch 390

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.