ArticleProceedings of the National Academy of Sciences of the United States of America2005
Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 136 citations in OpenAlex.
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- Evidence for biomolecular condensates formed by the Escherichia coli MatP protein in spatiotemporal regulation of the bacterial cell division cycle.International journal of biological macromolecules · 2025Article
- MoaB2, a newly identified transcription factor, binds to σJournal of bacteriology · 2024Article
- Assembly of SARS-CoV-2 nucleocapsid protein with nucleic acid.Nucleic acids research · 2024Article
- Studying Macromolecular Interactions of Cellular Machines by the Combined Use of Analytical Ultracentrifugation, Light Scattering, and Fluorescence Spectroscopy Methods.Advances in experimental medicine and biology · 2024Article
- Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.bioRxiv : the preprint server for biology · 2023Article
- AAV analysis by sedimentation velocity analytical ultracentrifugation: beyond empty and full capsids.European biophysics journal : EBJ · 2023Article
- Best Practices for Aggregate Quantitation of Antibody Therapeutics by Sedimentation Velocity Analytical Ultracentrifugation.Journal of pharmaceutical sciences · 2022Review
- Biophysical characterization of the complex between the iron-responsive transcription factor Fep1 and DNA.European biophysics journal : EBJ · 2021Article
- Biomolecular interactions of ultrasmall metallic nanoparticles and nanoclusters.Nanoscale advances · 2021Review
- Analytical Ultracentrifugation (AUC): An Overview of the Application of Fluorescence and Absorbance AUC to the Study of Biological Macromolecules.Current protocols in molecular biology · 2020Article
- Reversible regulation of conjugation of Bacillus subtilis plasmid pLS20 by the quorum sensing peptide responsive anti-repressor RappLS20.Nucleic acids research · 2020Article
- Characterization and Control of Dynamic Rearrangement in a Self-Assembled Antibody Carrier.Biomacromolecules · 2020Article
- Oligomerization of RIG-I and MDA5 2CARD domains.Protein science : a publication of the Protein Society · 2020Article
- A multiwavelength emission detector for analytical ultracentrifugation.Nanoscale advances · 2019Article
- Novel regulatory mechanism of establishment genes of conjugative plasmids.Nucleic acids research · 2018Article
- Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity.Nature communications · 2018Article
- Precise determination of protein extinction coefficients under native and denaturing conditions using SV-AUC.European biophysics journal : EBJ · 2018Article
- Structural insights into the mechanism of action of a biparatopic anti-HER2 antibody.The Journal of biological chemistry · 2018Article
- Analytical ultracentrifugation in structural biology.Biophysical reviews · 2018Review
17 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Protein interactions can promote the reversible assembly of multiprotein complexes, which have been identified as critical elements in many regulatory processes in cells. The biophysical characterization of assembly products, their number and stoichiometry, and the dynamics of their interactions in solution can be very difficult. A classical first-principle approach for the study of purified proteins and their interactions is sedimentation velocity analytical ultracentrifugation. This approach allows one to distinguish different protein complexes based on their migration in the centrifugal field without isolating reversibly formed complexes from the individual components. An important existing limitation for systems with multiple components and assembly products is the identification of the species associated with the observed sedimentation rates. We developed a computational approach for integrating multiple optical signals into the sedimentation coefficient distribution analysis of components, which combines the size-dependent hydrodynamic separation with discrimination of the extinction properties of the sedimenting species. This approach allows one to deduce the stoichiometry and to assign the identity of the assembly products without prior assumptions of the number of species and the nature of their interaction. Although chromophoric labels may be used to enhance the spectral resolution, we demonstrate the ability to work label-free for three-component protein mixtures. We observed that the spectral discrimination can synergistically enhance the hydrodynamic resolution. This method can take advantage of differences in the absorbance spectra of interacting solution components, for example, for the study of protein-protein, protein-nucleic acid or protein-small molecule interactions, and can determine the size, hydrodynamic shape, and stoichiometry of multiple complexes in solution.
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