Average quantities accessible to the analysis of sedimentation equilibrium data for self-association systems
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Updated: Oct 21, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Abstract:
This paper shows that analysis of sedimentation equilibrium data, searching for average molecular weights, gives quantities which are dependent on the total protein concentration of the samples, while knowledge of the molecular weight of the monomeric subunits allows a more meaningful search for the concentrations of the individual polymeric components of the system. From these the various average molecular weights can be construed, and the various dissociation equilibrium constants evaluated. Also, in this paper considerations are proposed on the meaning of nonideality terms in associating systems and possible ways for estimating them. As an example the proposed procedures have been applied to measurements of sedimentation equilibrium in carbonmonoxyhemoglobin.
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