ArticleBiophysical journal2005
Protein self-association induced by macromolecular crowding: a quantitative analysis by magnetic relaxation dispersion.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 83 citations in OpenAlex.
- Dynamic Cytoplasm: A Physical Regulator of Enzymatic Function.Biochemistry · 2025Review
- Effects of Molecular Crowding on the Structural, Dynamic, and Functional Properties of Biological Macromolecules: A General Overview.Sub-cellular biochemistry · 2025Review
- Novel insight into mechanisms of ROS1 catalytic activation via loss of the extracellular domain.Scientific reports · 2024Article
- Structural Refolding and Thermal Stability of Myoglobin in the Presence of Mixture of Crowders: Importance of Various Interactions for Protein Stabilization in Crowded Conditions.Molecules (Basel, Switzerland) · 2021Article
- Liquid-Liquid Phase Separation in Crowded Environments.International journal of molecular sciences · 2020Review
- Macromolecular Crowding In Vitro, In Vivo, and In Between.Trends in biochemical sciences · 2016Review
- Article
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
- Protein-protein interactions in a crowded environment.Biophysical reviews · 2013Review
- Formation of protein complexes in crowded environments--from in vitro to in vivo.FEBS letters · 2013Review
- Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling.FEBS letters · 2013Review
- Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents.Biophysical journal · 2012Article
- Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands.The Journal of biological chemistry · 2012Article
- Generalized fundamental measure theory for atomistic modeling of macromolecular crowding.Physical review. E, Statistical, nonlinear, and soft matter physics · 2010Article
- Protein adsorption and transport in dextran-modified ion-exchange media. I: adsorption.Journal of chromatography. A · 2009Article
- Common crowding agents have only a small effect on protein-protein interactions.Biophysical journal · 2009Article
- Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions.Journal of the American Chemical Society · 2009Article
- Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxin.Biophysical journal · 2009Article
- Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences.Annual review of biophysics · 2008Review
- A high-throughput method for detection of protein self-association and second virial coefficient using size-exclusion chromatography through simultaneous measurement of concentration and scattered light intensity.Pharmaceutical research · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the presence of high concentrations of inert macromolecules, the self-association of proteins is strongly enhanced through an entropic, excluded-volume effect variously called macromolecular crowding or depletion attraction. Despite the predicted large magnitude of this universal effect and its far-reaching biological implications, few experimental studies of macromolecular crowding have been reported. Here, we introduce a powerful new technique, fast field-cycling magnetic relaxation dispersion, for investigating crowding effects on protein self-association equilibria. By recording the solvent proton spin relaxation rate over a wide range of magnetic field strengths, we determine the populations of coexisting monomers and decamers of bovine pancreatic trypsin inhibitor in the presence of dextran up to a macromolecular volume fraction of 27%. Already at a dextran volume fraction of 14%, we find a 30-fold increase of the decamer population and 510(5)-fold increase of the association constant. The analysis of these results, in terms of a statistical-mechanical model that incorporates polymer flexibility as well as the excluded volume of the protein, shows that the dramatic enhancement of bovine pancreatic trypsin inhibitor self-association can be quantitatively rationalized in terms of hard repulsive interactions.
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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.