Evidence map›Paper›PMID 23561534›Full record

ArticleBiophysical journal2013

The shape of protein crowders is a major determinant of protein diffusion.

Jessica Balbo, Paolo Mereghetti, Dirk-Peter Herten, Rebecca C Wade

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 91 citations in OpenAlex.

  1. Lipoprotein diffusion in dense yolk plasma is governed by softness, hydrodynamics, and caging: Insights from MHz-XPCS.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
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  13. Parameter Reliability and Understanding Enzyme Function.Molecules (Basel, Switzerland) · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Evolutionary drivers of protein shape.Scientific reports · 2019
    Article
  19. Dynamic cluster formation determines viscosity and diffusion in dense protein solutions.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. 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

4 authors at 1 institution in 2 countries.

Jessica BalboCellNetworks Cluster and Physikalisch-Chemisches Institut, Heidelberg University, Heidelberg, Germany.
Paolo Mereghetti
Dirk-Peter Herten
Rebecca C Wade
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As a model for understanding how molecular crowding influences diffusion and transport of proteins in cellular environments, we combined experimental and theoretical approaches to study the diffusion of proteins in highly concentrated protein solutions. Bovine serum albumin and γ-Globulin were chosen as molecular crowders and as tracers. These two proteins are representatives of the main types of plasma protein and have different shapes and sizes. Solutions consisting of one or both proteins were studied. The self-diffusion coefficients of the fluorescently labeled tracer proteins were measured by means of fluorescence correlation spectroscopy at a total protein concentration of up to 400 g/L. γ-Globulin is found to have a stronger influence as a crowder on the tracer self-diffusion coefficient than Bovine serum albumin. Brownian dynamics simulations show that the excluded volume and the shape of the crowding protein have a significantly stronger influence on translational and rotational diffusion coefficients, as well as transient oligomerization, than hydrodynamic or direct interactions. Anomalous subdiffusion, which is not observed at the experimental fluorescence correlation spectroscopy timescales (>100 μs), appears only at very short timescales (<1 μs) in the simulations due to steric effects of the proteins. We envision that the combined experimental and computational approach employed here can be developed to unravel the different biophysical contributions to protein motion and interaction in cellular environments by systematically varying protein properties such as molecular weight, size, shape, and electrostatic interactions.

Indexed as

AnimalsCattleDiffusiongamma-GlobulinsHydrodynamicsMolecular Dynamics SimulationMolecular WeightRotationSerum Albumin, Bovinegamma-GlobulinsSerum Albumin, Bovine

Identifiers

PMID23561534
PMCPMC3617426
OpenAlexW2039461517

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.