Evidence map›Paper›PMID 31721348›Full record

ReviewProtein science : a publication of the Protein Society2020

Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry.

Edgar A Hodge, Mark A Benhaim, Kelly K Lee

Open access · greenAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
6.6field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 126 citations in OpenAlex.

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  15. Conformational dynamics underlying atypical chemokine receptor 3 activation.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

3 authors at 1 institution in 1 country.

Edgar A HodgeDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington.
Mark A BenhaimDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington.ORCID 0000-0003-2906-5599
Kelly K LeeDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington.
University of Washington · US

Funding

TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
Structural and dynamic traits underlying phenotypic variation in HIV-1 EnvR01AI140868 · NIAID · UNIVERSITY OF WASHINGTON · PI Kelly Keisen Lee · 2019 to 2026
$5.3M
Waters ACQUITY UPLC M-Class with NanoLockSpray ionization sourceR01GM099989 · NIGMS · UNIVERSITY OF WASHINGTON · PI LEE, KELLY KEISEN · 2012 to 2020
$3.5M
NIAID NIH HHS R01 AI140868NIGMS NIH HHS R01 GM099989NIGMS NIH HHS T32 GM008268NIH HHS T32GM008268-27
6 · The paper itself

Abstract

Much of our understanding of protein structure and mechanistic function has been derived from static high-resolution structures. As structural biology has continued to evolve it has become clear that high-resolution structures alone are unable to fully capture the mechanistic basis for protein structure and function in solution. Recently Hydrogen/Deuterium-exchange Mass Spectrometry (HDX-MS) has developed into a powerful and versatile tool for structural biologists that provides novel insights into protein structure and function. HDX-MS enables direct monitoring of a protein's structural fluctuations and conformational changes under native conditions in solution even as it is carrying out its functions. In this review, we focus on the use of HDX-MS to monitor these dynamic changes in proteins. We examine how HDX-MS has been applied to study protein structure and function in systems ranging from large, complex assemblies to intrinsically disordered proteins, and we discuss its use in probing conformational changes during protein folding and catalytic function. STATEMENT FOR A BROAD AUDIENCE: The biophysical and structural characterization of proteins provides novel insight into their functionalities. Protein motions, ranging from small scale local fluctuations to larger concerted structural rearrangements, often determine protein function. Hydrogen/Deuterium-exchange Mass Spectrometry (HDX-MS) has proven a powerful biophysical tool capable of probing changes in protein structure and dynamic protein motions that are often invisible to most other techniques.

Indexed as

Hydrogen Deuterium Exchange-Mass SpectrometryIntrinsically Disordered ProteinsMolecular Dynamics SimulationProtein ConformationIntrinsically Disordered Proteinsconformational switchingconformational transitionshydrogen/deuterium-exchange mass spectrometry (HDX-MS)intrinsic disorderstructural dynamicsstructural rearrangements

Identifiers

PMID31721348
PMCPMC7096709
OpenAlexW2983202177

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.