ArticleNature protocols2017
Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.
Article in Nature protocols, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
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- The intrinsically disordered AB region: a key modulator of the molecular properties of human RXRγ.Cell communication and signaling : CCS · 2025Article
- Development of an advanced multiwavelength emission detector for the analytical ultracentrifuge.Nanoscale advances · 2024Article
- The IRE1β-mediated unfolded protein response is repressed by the chaperone AGR2 in mucin producing cells.The EMBO journal · 2024Article
- Antifouling strategies for electrochemical sensing in complex biological media.Mikrochimica acta · 2024Review
- The Thermodynamic Fingerprints of Ultra-Tight Nanobody-Antigen Binding Probed via Two-Color Single-Molecule Coincidence Detection.International journal of molecular sciences · 2023Article
- E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity.Molecular cell · 2023Article
- Hierarchical assembly of the MLL1 core complex regulates H3K4 methylation and is dependent on temperature and component concentration.The Journal of biological chemistry · 2023Article
- Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.Nature microbiology · 2022Article
- Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021Review
- Characterization of DNA-protein complexes by nanoparticle tracking analysis and their association with systemic lupus erythematosus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- An essential role of the autophagy activating kinase ULK1 in snRNP biogenesis.Nucleic acids research · 2021Article
- On the utility of fluorescence-detection analytical ultracentrifugation in probing biomolecular interactions in complex solutions: a case study in milk.European biophysics journal : EBJ · 2020Article
- 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
- Quantitative Analysis of Protein Self-Association by Sedimentation Velocity.Current protocols in protein science · 2020Article
- Visualizing the functional 3D shape and topography of long noncoding RNAs by single-particle atomic force microscopy and in-solution hydrodynamic techniques.Nature protocols · 2020Article
- Efficient data acquisition with three-channel centerpieces in sedimentation velocity.Analytical biochemistry · 2019Article
- Identification of the periplasmic DNA receptor for natural transformation of Helicobacter pylori.Nature communications · 2019Article
- Nucleic acid-induced dimerization of HIV-1 Gag protein.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Sedimentation velocity (SV) analytical ultracentrifugation (AUC) is a classic technique for the real-time observation of free macromolecular migration in solution driven by centrifugal force. This enables the analysis of macromolecular mass, shape, size distribution, and interactions. Although traditionally limited to determination of the sedimentation coefficient and binding affinity of proteins in the micromolar range, the implementation of modern detection and data analysis techniques has resulted in marked improvements in detection sensitivity and size resolution during the past decades. Fluorescence optical detection now permits the detection of recombinant proteins with fluorescence excitation at 488 or 561 nm at low picomolar concentrations, allowing for the study of high-affinity protein self-association and hetero-association. Compared with other popular techniques for measuring high-affinity protein-protein interactions, such as biosensing or calorimetry, the high size resolution of complexes at picomolar concentrations obtained with SV offers a distinct advantage in sensitivity and flexibility of the application. Here, we present a basic protocol for carrying out fluorescence-detected SV experiments and the determination of the size distribution and affinity of protein-antibody complexes with picomolar K
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