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Biophysical Chemistry|July 2, 2003
Allowance for thermodynamic non-ideality in the characterization of protein self-association by frontal exclusion chromatography: hemoglobin revisitedDonald J Winzor, Peter R WillsJournal of Molecular Recognition : JMR|August 10, 2006
Interpretation of the temperature dependence of equilibrium and rate constantsDonald J Winzor, Craig M JacksonBiophysical Chemistry|May 10, 2011
Allowance for thermodynamic nonideality in the characterization of protein interactions by spectral techniquesPeter R Wills, Donald J WinzorMolecular Biosystems|September 29, 2011
Sedimentation velocity of intrinsically disordered proteins: what information can we actually obtain?David J Scott, Donald J WinzorJournal of Molecular Recognition : JMR|August 4, 2011
Reassessment of the size of the supermolecular state of Dishevelled-3Trushar R Patel, Donald J WinzorMethods in Enzymology|September 29, 2015
Characterization of Intrinsically Disordered Proteins by Analytical UltracentrifugationDavid J Scott, Donald J WinzorAnalytical Biochemistry|June 2, 2007
Characterization of weak protein dimerization by direct analysis of sedimentation equilibrium distributions: the INVEQ approachDonald J Winzor, Peter R WillsBiophysical Reviews|June 19, 2026
Correction to: A quest for greater thermodynamic rigour in the quantitative characterization of protein self-association by direct assessment of sedimentation equilibrium distributionsDonald J Winzor, Peter R WillsBiophysical Reviews|June 19, 2026
A quest for greater thermodynamic rigour in the quantitative characterization of protein self-association by direct assessment of sedimentation equilibrium distributionsDonald J Winzor, Peter R WillsBiophysical Chemistry|May 26, 2019
Quantitative interpretation of isopiestic measurements on aqueous solutions: Urea revisitedDonald J Winzor, Peter R WillsPageof 8