Evidence map›Paper›PMID 37573815›Full record

ReviewCurrent opinion in structural biology2023

Direct measurements of biomolecular electrostatics through experiments.

Junji Iwahara, B Montgomery Pettitt, Binhan Yu

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Cysteine thiol-to-sulfonate oxidation induces unfolding for the functional switching of the extracellular HMGB1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Transient helices with functional roles.Biophysical journal · 2024
    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.

Junji IwaharaDepartment of Biochemistry & Molecular Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA. Electronic address: j.iwahara@utmb.edu.
B Montgomery PettittDepartment of Biochemistry & Molecular Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA.
Binhan YuDepartment of Biochemistry & Molecular Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA.

Funding

Theory of Proteins and Peptides in SolutionR01GM037657 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI PETTITT, BERNARD MONTGOMERY · 1988 to 2023
$5.5M
Dynamics of DNA scanning and recognition by transcription factorsR35GM130326 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI Junji Iwahara · 2019 to 2026
$4.2M
NIGMS NIH HHS R01 GM037657NIGMS NIH HHS R35 GM130326
6 · The paper itself

Abstract

Biomolecular electrostatics has been a subject of computational investigations based on 3D structures. This situation is changing because emerging experimental tools allow us to quantitatively investigate biomolecular electrostatics without any use of structure information. Now, electrostatic potentials around biomolecules can directly be measured for many residues simultaneously by nuclear magnetic resonance (NMR) spectroscopy. This NMR method can be used to study electrostatic aspects of various processes, including macromolecular association and liquid-liquid phase separation. Applications to structurally flexible biomolecules such as intrinsically disordered proteins are particularly useful. The new tools also facilitate examination of theoretical models and methods for biomolecular electrostatics.

Indexed as

Intrinsically Disordered ProteinsMagnetic Resonance SpectroscopyModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationStatic ElectricityIntrinsically Disordered Proteins

Identifiers

PMID37573815
PMCPMC10947535

What OpenQuestion holds

Textmetadata
LicenceTDM
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.