Evidence map›Paper›PMID 19791823›Full record

ArticleThe journal of physical chemistry. B2009

Translational and rotational diffusion of a small globular protein under crowded conditions.

Conggang Li, Yaqiang Wang, Gary J Pielak

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

38 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Biomolecular phase separation through the lens of sodium-23 NMR.Protein science : a publication of the Protein Society · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Diffusive protein interactions in human versus bacterial cells.Current research in structural biology · 2020
    Article
  12. Liquid Metastable Precursors of Ibuprofen as Aqueous Nucleation Intermediates.Angewandte Chemie (International ed. in English) · 2019
    Article
  13. Article
  14. Whole-Cell Models and Simulations in Molecular Detail.Annual review of cell and developmental biology · 2019
    Review
  15. Review
  16. Article
  17. Measuring translational diffusion ofEuropean biophysics journal : EBJ · 2018
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Conggang LiDepartment of Chemistry, Department of Biochemistry and Biophysics, and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
Yaqiang Wang
Gary J Pielak
University of North Carolina at Chapel Hill · US

Funding

NIH Director's Pioneer AwardDP1OD000783 · OD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PIELAK, GARY JOSEPH · 2006 to 2010
$3.7M
NCCDPHP CDC HHS 5DP10D783NIH HHS DP1 OD000783
6 · The paper itself

Abstract

Protein-protein interaction is the fundamental step of biological signal transduction. Interacting proteins find each other by diffusion. To gain insight into diffusion under the crowded conditions found in cells, we used nuclear magnetic resonance spectroscopy (NMR) to measure the effects of solvent additives on the translational and rotational diffusion of the 7.4 kDa globular protein, chymotrypsin inhibitor 2. The additives were glycerol and the macromolecular crowding agent, polyvinyl pyrrolidone (PVP). Both translational diffusion and rotational diffusion decrease with increasing solution viscosity. For glycerol, the decrease obeys the Stokes-Einstein and Stokes-Einstein Debye laws. Three types of deviation are observed for PVP: the decrease in diffusion with increased viscosity is less than predicted, this negative deviation is greater for rotational diffusion, and the negative deviation increases with increasing PVP molecular weight. We discuss our results in terms of other studies on the effects of macromolecules on globular protein diffusion.

Indexed as

DiffusionGlycerolMolecular WeightNuclear Magnetic Resonance, BiomolecularPeptidesPlant ProteinsPolyvinylsPyrrolidinesRotationSignal TransductionSolventsViscositychymotrypsin inhibitor 2GlycerolPeptidesPlant Proteinspoly(N-vinylpyrrolidine)PolyvinylsPyrrolidinesSolvents

Identifiers

PMID19791823
PMCPMC2774775
OpenAlexW2078016208

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.