Evidence map›Paper›PMID 30944216›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Relative interfacial cleavage energetics of protein complexes revealed by surface collisions.

Sophie R Harvey, Justin T Seffernick, Royston S Quintyn, Yang Song, Yue Ju, Jing Yan, Aniruddha N Sahasrabuddhe, Andrew Norris, Mowei Zhou, Edward J Behrman and 2 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 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

12 authors.

Sophie R HarveyDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.ORCID 0000-0003-0763-8173
Justin T SeffernickDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Royston S QuintynDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Yang SongDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Yue JuDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Jing YanDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Aniruddha N SahasrabuddheDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Andrew NorrisDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Mowei ZhouDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Edward J BehrmanDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Steffen LindertDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210; lindert.1@osu.edu wysocki.11@osu.edu.
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210; lindert.1@osu.edu wysocki.11@osu.edu.ORCID 0000-0003-0495-2538

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI SOMOGYI, ARPAD · 2018 to 2022
$7.6M
Development of Surface-Induced Dissociation Ion Mobility MS, a Structrl Biol ToolR01GM113658 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2015 to 2018
$1.1M
NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM113658
6 · The paper itself

Abstract

To fulfill their biological functions, proteins must interact with their specific binding partners and often function as large assemblies composed of multiple proteins or proteins plus other biomolecules. Structural characterization of these complexes, including identification of all binding partners, their relative binding affinities, and complex topology, is integral for understanding function. Understanding how proteins assemble and how subunits in a complex interact is a cornerstone of structural biology. Here we report a native mass spectrometry (MS)-based method to characterize subunit interactions in globular protein complexes. We demonstrate that dissociation of protein complexes by surface collisions, at the lower end of the typical surface-induced dissociation (SID) collision energy range, consistently cleaves the weakest protein:protein interfaces, producing products that are reflective of the known structure. We present here combined results for multiple complexes as a training set, two validation cases, and four computational models. We show that SID appearance energies can be predicted from structures via a computationally derived expression containing three terms (number of residues in a given interface, unsatisfied hydrogen bonds, and a rigidity factor).

Indexed as

Computer SimulationHydrogen BondingMass SpectrometryProtein BindingProteinsSurface PropertiesProteinsnative mass spectrometryprotein complexprotein interactionsstructural biologysurface-induced dissociation

Identifiers

PMID30944216
PMCPMC6486728

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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.