Evidence map›Paper›PMID 34932911›Full record

ReviewAnnual review of biophysics2022

Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions.

Arthur Laganowsky, David E Clemmer, David H Russell

Abstract readReview
In one paragraph

Review in Annual review of biophysics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure and Stabilities of Solution and Gas Phase Protein Complexes.Journal of the American Society for Mass Spectrometry · 2024
    Article
  14. Temperature-Dependent TrimethylamineThe journal of physical chemistry. B · 2024
    Article
  15. Article
  16. Water Plays Key Roles in Stabilities of Wild Type and Mutant Transthyretin Complexes.Journal of the American Society for Mass Spectrometry · 2024
    Article
  17. Thermal Remodeling of Human HDL Particles Reveals Diverse Subspecies.Journal of the American Society for Mass Spectrometry · 2024
    Article
  18. Article
  19. Article
  20. Stability of End-to-End Base Stacking Interactions in Highly Concentrated DNA Solutions.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
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.

Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, Texas, USA; email: alaganowsky@chem.tamu.edu, russell@chem.tamu.edu.
David E ClemmerDepartment of Chemistry, Indiana University, Bloomington, Indiana, USA; email: clemmer@indiana.edu.
David H RussellDepartment of Chemistry, Texas A&M University, College Station, Texas, USA; email: alaganowsky@chem.tamu.edu, russell@chem.tamu.edu.

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
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
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
Innovative Native Ion Mobility Approaches for Transformational Measurements in Structural BiologyR01GM138863 · NIGMS · TEXAS A&M UNIVERSITY · PI CLOWERS, BRIAN, LAGANOWSKY, ARTHUR D · 2020 to 2023
$1.2M
Developing new tools to probe membrane protein-lipid interactions for biomedical applicationsR01GM139876 · NIGMS · TEXAS A&M UNIVERSITY · PI LAGANOWSKY, ARTHUR D · 2021 to 2024
$1.2M
NIGMS NIH HHS DP2 GM123486NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM121751NIGMS NIH HHS R01 GM138863NIGMS NIH HHS R01 GM139876
6 · The paper itself

Abstract

The structures and conformational dynamics of proteins, protein complexes, and their noncovalent interactions with other molecules are controlled specifically by the Gibbs free energy (entropy and enthalpy) of the system. For some organisms, temperature is highly regulated, but the majority of biophysical studies are carried out at room, nonphysiological temperature. In this review, we describe variable-temperature electrospray ionization (vT-ESI) mass spectrometry (MS)-based studies with unparalleled sensitivity, dynamic range, and selectivity for studies of both cold- and heat-induced chemical processes. Such studies provide direct determinations of stabilities, reactivities, and thermodynamic measurements for native and non-native structures of proteins and protein complexes and for protein-ligand interactions. Highlighted in this review are vT-ESI-MS studies that reveal 40 different conformers of chymotrypsin inhibitor 2, a classic two-state (native → unfolded) unfolder, and thermochemistry for a model membrane protein system binding lipid and its regulatory protein.

Indexed as

Protein FoldingSpectrometry, Mass, Electrospray IonizationLigandsTemperatureThermodynamicsLigandsnative mass spectrometryprotein foldingprotein–ligand interactionsthermodynamicsvariable-temperature electrospray ionization

Identifiers

PMID34932911
PMCPMC9086101

What OpenQuestion holds

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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.