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Journal of Chromatography|August 11, 1989
Biospecific interactions: their quantitative characterization and use for solute purificationD J Winzor, J De JerseyBiophysical Chemistry|December 31, 1986
Effects of thermodynamic nonideality on protein interactions. Equivalence of interpretations based on excluded volume and preferential solvationD J Winzor, P R WillsArchives of Biochemistry and Biophysics|October 1, 1984
Quantitative affinity chromatography: further developments in the analysis of experimental results from column chromatography and partition equilibrium studiesP J Hogg, D J WinzorArchives of Biochemistry and Biophysics|April 1, 1987
Further probes into quantitative aspects of competitive binding assays: allowance for effects of antigen multivalency in immunoassaysP J Hogg, D J WinzorBiophysical Chemistry|September 12, 2001
Studies of solute self-association by sedimentation equilibrium: allowance for effects of thermodynamic non-ideality beyond the consequences of nearest-neighbor interactionsP R Wills, D J WinzorAnalytical Biochemistry|May 1, 1996
Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technologyD J O'Shannessy, D J WinzorJournal of Chromatography. B, Biomedical Sciences and Applications|October 29, 1998
Potential of biosensor technology for the characterization of interactions by quantitative affinity chromatographyD R Hall, D J WinzorBiochemistry|October 5, 2001
Interpretation of the reversible inhibition of adenosine deaminase by small cosolutes in terms of molecular crowdingT G Lonhienne, D J WinzorBiochimica Et Biophysica Acta|March 23, 1988
Allowance for effects of electrostatic repulsion on protein dimerizationP M Agapow, D J WinzorPageof 24