ArticleActa crystallographica. Section D, Biological crystallography2015
Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 185 citations in OpenAlex.
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- The structure of the extracellular domains of human interleukin 11α receptor reveals mechanisms of cytokine engagement.The Journal of biological chemistry · 2020Article
- Structural basis of cell-surface signaling by a conserved sigma regulator in Gram-negative bacteria.The Journal of biological chemistry · 2020Article
- 4S-Hydroxylation of Insulin at ProB28 Accelerates Hexamer Dissociation and Delays Fibrillation.Journal of the American Chemical Society · 2017Article
- Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Integration and global analysis of isothermal titration calorimetry data for studying macromolecular interactions.Nature protocols · 2016Article
- Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.The Journal of biological chemistry · 2016Article
- On the acquisition and analysis of microscale thermophoresis data.Analytical biochemistry · 2016Article
- SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Methods (San Diego, Calif.) · 2015Review
- In pursuit of an accurate spatial and temporal model of biomolecules at the atomistic level: a perspective on computer simulation.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocity.Analytical chemistry · 2014Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Reversible macromolecular interactions are ubiquitous in signal transduction pathways, often forming dynamic multi-protein complexes with three or more components. Multivalent binding and cooperativity in these complexes are often key motifs of their biological mechanisms. Traditional solution biophysical techniques for characterizing the binding and cooperativity are very limited in the number of states that can be resolved. A global multi-method analysis (GMMA) approach has recently been introduced that can leverage the strengths and the different observables of different techniques to improve the accuracy of the resulting binding parameters and to facilitate the study of multi-component systems and multi-site interactions. Here, GMMA is described in the software SEDPHAT for the analysis of data from isothermal titration calorimetry, surface plasmon resonance or other biosensing, analytical ultracentrifugation, fluorescence anisotropy and various other spectroscopic and thermodynamic techniques. The basic principles of these techniques are reviewed and recent advances in view of their particular strengths in the context of GMMA are described. Furthermore, a new feature in SEDPHAT is introduced for the simulation of multi-method data. In combination with specific statistical tools for GMMA in SEDPHAT, simulations can be a valuable step in the experimental design.
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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 Socratic graph.