Evidence map›Paper›PMID 35485934›Full record

ArticleThe journal of physical chemistry letters2022

Interplay of Affinity and Surface Tethering in Protein Recognition.

Ali Imran, Brandon S Moyer, Aaron J Wolfe, Michael S Cosgrove, Dmitrii E Makarov, Liviu Movileanu

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

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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

6 authors.

Ali ImranDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United States.
Brandon S MoyerIchor Life Sciences, Inc., 2651 US Route 11, LaFayette, New York 13084, United States.
Aaron J WolfeDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United States.
Michael S CosgroveDepartment of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, 4249 Weiskotten Hall, 766 Irving Avenue, Syracuse, New York 13210, United States.
Dmitrii E MakarovDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0002-8421-1846
Liviu MovileanuDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United States.ORCID 0000-0002-2525-3341

Funding

Molecular Mechanisms for the Assembly and Regulation of the MLL1 Core ComplexR01CA140522 · NCI · UPSTATE MEDICAL UNIVERSITY · PI COSGROVE, MICHAEL S. · 2010 to 2019
$3.6M
Disentanglement of the MLL-WDR5 Protein-Protein Recognition EventsR01GM129429 · NIGMS · SYRACUSE UNIVERSITY · PI MOVILEANU, LIVIU · 2018 to 2021
$1.3M
NCI NIH HHS R01 CA140522NIGMS NIH HHS R01 GM129429
6 · The paper itself

Abstract

Surface-tethered ligand-receptor complexes are key components in biological signaling and adhesion. They also find increasing utility in single-molecule assays and biotechnological applications. Here, we study the real-time binding kinetics between various surface-immobilized peptide ligands and their unrestrained receptors. A long peptide tether increases the association of ligand-receptor complexes, experimentally proving the fly casting mechanism where the disorder accelerates protein recognition. On the other hand, a short peptide tether enhances the complex dissociation. Notably, the rate constants measured for the same receptor, but under different spatial constraints, are strongly correlated to one another. Furthermore, this correlation can be used to predict how surface tethering on a ligand-receptor complex alters its binding kinetics. Our results have immediate implications in the broad areas of biomolecular recognition, intrinsically disordered proteins, and biosensor technology.

Indexed as

Intrinsically Disordered ProteinsKineticsLigandsPeptidesProtein BindingIntrinsically Disordered ProteinsLigandsPeptides

Identifiers

PMID35485934
PMCPMC9106920

What OpenQuestion holds

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LicenceCC BY
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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.