Evidence map›Paper›PMID 33904705›Full record

ArticleAnalytical chemistry2021

Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding.

Jacob W McCabe, Mehdi Shirzadeh, Thomas E Walker, Cheng-Wei Lin, Benjamin J Jones, Vicki H Wysocki, David P Barondeau, David E Clemmer, Arthur Laganowsky, David H Russell

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.1field-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

49 citing papers in PubMed, 88 citations in OpenAlex.

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  11. Hydration (HJournal of the American Chemical Society · 2025
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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

10 authors at 3 institutions in 1 country.

Jacob W McCabeDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0002-5022-2280
Mehdi ShirzadehDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0001-6306-9687
Thomas E WalkerDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
Cheng-Wei LinDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0002-6917-8953
Benjamin J JonesDepartment of Chemistry, Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0002-6135-4377
Vicki H WysockiDepartment of Chemistry, Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0003-0495-2538
David P BarondeauDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0002-6422-9053
David E ClemmerDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.ORCID 0000-0003-4039-1360
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0001-5012-5547
David H RussellDepartment of Chemistry, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0003-0830-3914
Texas A&M University · USThe Ohio State University · USIndiana University Bloomington · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
Structure and Mechanism of the Human FE-S Cluster Assembly ComplexR01GM096100 · NIGMS · TEXAS A&M UNIVERSITY · PI BARONDEAU, DAVID P · 2011 to 2024
$3.5M
Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid bindingDP2GM123486 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI LAGANOWSKY, ARTHUR D · 2016 to 2016
$2.2M
Developing High-Resolution Ion Mobility Spectrometry-Charge Detection-Mass Spectrometry for Rapid Analysis in the Megadalton to Gigadalton RegimeR01GM131100 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., JARROLD, MARTIN F · 2019 to 2022
$2.1M
Development of high resolution mobility measurements for structural biologyR01GM121751 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., LAGANOWSKY, ARTHUR D · 2017 to 2020
$1.7M
NIGMS NIH HHS DP2 GM123486NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM096100NIGMS NIH HHS R01 GM121751NIGMS NIH HHS R01 GM131100
6 · The paper itself

Abstract

Stabilities and structure(s) of proteins are directly coupled to their local environment or Gibbs free energy landscape as defined by solvent, temperature, pressure, and concentration. Solution pH, ionic strength, cofactors, chemical chaperones, and osmolytes perturb the chemical potential and induce further changes in structure, stability, and function. At present, no single analytical technique can monitor these effects in a single measurement. Mass spectrometry and ion mobility-mass spectrometry play increasingly essential roles in studies of proteins, protein complexes, and even membrane protein complexes; however, with few exceptions, the effects of the solution temperature on the stability and structure(s) of analytes have not been thoroughly investigated. Here, we describe a new variable-temperature electrospray ionization (vT-ESI) source that utilizes a thermoelectric chip to cool and heat the solution contained within the static ESI emitter. This design allows for solution temperatures to be varied from ∼5 to 98 °C with short equilibration times (<2 min) between precisely controlled temperature changes. The performance of the apparatus for vT-ESI-mass spectrometry and vT-ESI-ion mobility-mass spectrometry studies of cold- and heat-folding reactions is demonstrated using ubiquitin and frataxin. Instrument performance for studies on temperature-dependent ligand binding is shown using the chaperonin GroEL.

Indexed as

ProteinsSpectrometry, Mass, Electrospray IonizationLigandsPhase TransitionTemperatureLigandsProteins

Identifiers

PMID33904705
PMCPMC8119373
OpenAlexW3157814829

What OpenQuestion holds

Textmetadata
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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.