ArticleProtein science : a publication of the Protein Society2004
Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Article
- Measuring the effects of macromolecular crowding on antibody function with biolayer interferometry.mAbs · 2019Article
- Toward an understanding of biochemical equilibria within living cells.Biophysical reviews · 2018Review
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Analysis of the size dependence of macromolecular crowding shows that smaller is better.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Phosphatidylserine and FVa regulate FXa structure.The Biochemical journal · 2014Article
- Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube.Biophysical reviews · 2013Review
- 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
- Dynamics-stability relationships in apo- and holomyoglobin: a combined neutron scattering and molecular dynamics simulations study.Biophysical journal · 2012Article
- Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria.Biophysical journal · 2010Article
- Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm.PLoS computational biology · 2010Article
- 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
- Protein self-association induced by macromolecular crowding: a quantitative analysis by magnetic relaxation dispersion.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The self-association equilibrium of a tracer protein, apomyoglobin (apoMb), in highly concentrated crowded solutions of ribonuclease A (RNase A) and human serum albumin (HSA), has been studied as a model system of protein interactions that occur in crowded macromolecular environments. The rotational diffusion of the tracer protein labeled with two different fluorescent dyes, 8-anilinonaphthalene-1-sulfonate and fluorescein isothiocyanate, was successfully recorded as a function of the two crowder concentrations in the 50-200 mg/mL range, using picosecond-resolved fluorescence anisotropy methods. It was found that apoMb molecules self-associate at high RNase A concentration to yield a flexible dimer. The apparent dimerization constant, which increases with RNase A concentration, could also be estimated from the fractional contribution of monomeric and dimeric species to the total fluorescence anisotropy of the samples. In contrast, an equivalent mass concentration of HSA does not result in tracer dimerization. This different effect of RNase A and HSA is much larger than that predicted from simple models based only on the free volume available to apoMb, indicating that additional, nonspecific interactions between tracer and crowder should come into play. The time-resolved fluorescence polarization methods described here are expected to be of general applicability to the detection and quantification of crowding effects in a variety of macromolecules of biological relevance.
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