THE DETERMINATION OF MONOMER–DIMER SELF-ASSOCIATION EQUILIBRIUM CONSTANTS IN DILUTE SOLUTIONS

1964 ◽  
Vol 42 (12) ◽  
pp. 2932-2935 ◽  
Author(s):  
S. N. Vinogradov

not available

2000 ◽  
Vol 39 (2) ◽  
pp. 197-223 ◽  
Author(s):  
CHRISTOPHER S. CLEVELAND ◽  
STEPHEN P. FEARNLEY ◽  
YUHONG HU ◽  
MARK E. WAGMAN ◽  
PAUL C. PAINTER ◽  
...  

2006 ◽  
Vol 41 (1) ◽  
pp. 21-27 ◽  
Author(s):  
A. González ◽  
L. Irusta ◽  
M.J. Fernández-Berridi ◽  
J.J. Iruin ◽  
T. Sierra ◽  
...  

1979 ◽  
Vol 34 (3) ◽  
pp. 369-374 ◽  
Author(s):  
M. Kunst ◽  
D. van Duijn ◽  
P. Bordewijk

Abstract Analysis of infrared hydroxyl multimer absorbances of dilute solutions of cholesterol in carbon tetrachloride as a function of the monomer absorbance strongly favours the interpretation of the association of this alcohol with a monomer-dimer-tetramer model up to a molar fraction of 0.012. This model also explains very well the concentration dependence of the apparent dipole moment. Equilibrium constants and dielectric parameters have been determined. Suggestions about the structure of the various associates are made.


Polymer ◽  
1996 ◽  
Vol 37 (21) ◽  
pp. 4753-4761 ◽  
Author(s):  
Michael M. Coleman ◽  
George J. Pehlert ◽  
Xiaoming Yang ◽  
John B. Stallman ◽  
Paul C. Painter

2003 ◽  
Vol 31 (5) ◽  
pp. 1010-1014 ◽  
Author(s):  
D.J. Winzor

This article reviews the progress of a personal endeavour to develop chromatography as a quantitative procedure for the determination of reaction stoichiometries and equilibrium constants governing protein interactions. As well as affording insight into an aspect of chromatography with which many protein chemists are unfamiliar, it shows the way in which minor adaptations of conventional chromatographic practices have rendered the technique one of the most powerful methods available for the characterization of interactions. That pathway towards quantification is followed from the introduction of frontal gel filtration for the study of protein self-association to the characterization of ligand binding by the biosensor variant of quantitative affinity chromatography.


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