Evidence map›Paper›PMID 21730176›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Protein self-diffusion in crowded solutions.

Felix Roosen-Runge, Marcus Hennig, Fajun Zhang, Robert M J Jacobs, Michael Sztucki, Helmut Schober, Tilo Seydel, Frank Schreiber

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
7.7field-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

80 citing papers in PubMed, 240 citations in OpenAlex.

  1. Non-Fickian diffusion within assemblies of the intrinsically disordered protein β-casein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. 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
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  10. Global warming risks dehydrating and inflaming human airways.Communications earth & environment · 2025
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  18. The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
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  19. Review
  20. Stacking Interactions and Flexibility of Human Telomeric Multimers.Journal of the American Chemical Society · 2023
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20 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 3 countries.

Felix Roosen-RungeInstitut für Angewandte Physik, Universität Tübingen, 72076 Tübingen, Germany.
Marcus Hennig
Fajun Zhang
Robert M J Jacobs
Michael Sztucki
Helmut Schober
Tilo Seydel
Frank Schreiber
University of Tübingen · DEInstitut Laue-Langevin · FREuropean Synchrotron Radiation Facility · FRUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macromolecular crowding in biological media is an essential factor for cellular function. The interplay of intermolecular interactions at multiple time and length scales governs a fine-tuned system of reaction and transport processes, including particularly protein diffusion as a limiting or driving factor. Using quasielastic neutron backscattering, we probe the protein self-diffusion in crowded aqueous solutions of bovine serum albumin on nanosecond time and nanometer length scales employing the same protein as crowding agent. The measured diffusion coefficient D(ϕ) strongly decreases with increasing protein volume fraction ϕ explored within 7% ≤ ϕ ≤ 30%. With an ellipsoidal protein model and an analytical framework involving colloid diffusion theory, we separate the rotational D(r)(ϕ) and translational D(t)(ϕ) contributions to D(ϕ). The resulting D(t)(ϕ) is described by short-time self-diffusion of effective spheres. Protein self-diffusion at biological volume fractions is found to be slowed down to 20% of the dilute limit solely due to hydrodynamic interactions.

Indexed as

Models, ChemicalDiffusionMacromolecular SubstancesNeutron DiffractionRotationSerum Albumin, BovineWaterMacromolecular SubstancesSerum Albumin, BovineWater

Identifiers

PMID21730176
PMCPMC3142006
OpenAlexW1985229185

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.