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Conformational studies of BSA using laser light scattering
Author(s) -
Harvey John D.,
Geddes Robert,
Wills Peter R.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180912
Subject(s) - chemistry , dimer , bovine serum albumin , hydrodynamic radius , light scattering , monomer , scattering , diffusion , static light scattering , molecule , analytical chemistry (journal) , crystallography , chromatography , aqueous solution , thermodynamics , optics , micelle , organic chemistry , polymer , physics
The usefulness of laser light scattering as a technique for determining protein conformation has been investigated by studying the self‐association and drug binding of bovine serum albumin (BSA). The diffusion coefficients of BSA monomers and dimers have been measured and the ratio of these two quantities indicates that in the dimer, the subunit separation is 2.2 times the monomeric hydrodynamic radius. The binding of salicylate to BSA causes an increase in its diffusion coefficient corresponding to a reduction in the frictional drag of the solvent on the protein molecules. It has been found that data obtained using laser light scattering may be interpreted confidently only when proper care has been taken in sample preparation and the scattered intensity autocorrelation function has been appropriately analyzed.