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Transient Incomplete Separation Facilitates Finding Accurate Equilibrium Dissociation Constant of Protein-Small Molecule Complex.
Sisavath, Nicolas; Rukundo, Jean-Luc; Le Blanc, J C Yves; Galievsky, Victor A; Bao, Jiayin; Kochmann, Sven; Stasheuski, Alexander S; Krylov, Sergey N.
Afiliación
  • Sisavath N; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
  • Rukundo JL; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
  • Le Blanc JCY; SCIEX, Concord, Ontario, L4K 4V8, Canada.
  • Galievsky VA; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
  • Bao J; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
  • Kochmann S; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
  • Stasheuski AS; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
  • Krylov SN; Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, M3J 1P3, Canada.
Angew Chem Int Ed Engl ; 58(20): 6635-6639, 2019 05 13.
Article en En | MEDLINE | ID: mdl-30901510
Current practical methods for finding the equilibrium dissociation constant, Kd , of protein-small molecule complexes have inherent sources of inaccuracy. Introduced here is "accurate constant via transient incomplete separation" (ACTIS), which appears to be free of inherent sources of inaccuracy. Conceptually, a short plug of the pre-equilibrated protein-small molecule mixture is pressure-propagated in a capillary, causing fast transient incomplete separation of the complex from the unbound small molecule. A superposition of signals from these two components is measured near the capillary exit and used to calculate a fraction of unbound small molecule, which, in turn, is used to calculate Kd . Herein the validity of ACTIS is proven theoretically, its accuracy is verified by computer simulation, and its practical use is demonstrated. ACTIS has the potential to become a reference-standard method for determining Kd  values of protein-small molecule complexes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Electroforesis Capilar Tipo de estudio: Diagnostic_studies Idioma: En Revista: Angew Chem Int Ed Engl Año: 2019 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Alemania
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Electroforesis Capilar Tipo de estudio: Diagnostic_studies Idioma: En Revista: Angew Chem Int Ed Engl Año: 2019 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Alemania