Title
Light-scattering by bovine alpha-crystallin proteins in solution : hydrodynamic structure and interparticle interaction Light-scattering by bovine alpha-crystallin proteins in solution : hydrodynamic structure and interparticle interaction
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
New York, N.Y. ,
Subject
Physics
Biology
Source (journal)
Biophysical journal. - New York, N.Y.
Volume/pages
66(1994) :3 Part 1 , p. 861-872
ISSN
0006-3495
ISI
A1994MZ35300033
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
We have studied diluted bovine eye lens alpha-crystallin solutions by using light scattering. The protein particles were modeled as hard spheres, showing electrostatic repulsion, due to surplus electric charges, and weak attractive interaction. The repulsive potential V-R is defined by the radius of the particles, the Debye length K-1, and the number of charges at the Gouy layer; the attractive potential has been described by the London-van der Waals potential and is defined by the Hamaker constant A. We have used the diluted gas approximation and the one component macrofluid model to relate the experimental static factor K-1 to the theoretical expression of the interaction potential V(x). This resulted in a Hamaker constant A of 0.06 +/- 0.01 KBT and an effective charge q ranging from 18 +/- 1 at low ionic strength (Omega = 0.0022 M) to 50 +/- 5 at high ionic strength(Omega = 0.1472M).
Full text (open access)
https://repository.uantwerpen.be/docman/irua/56d24d/4409.pdf
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