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Conformational studies of BSA using laser light scattering

✍ Scribed by John D. Harvey; Robert Geddes; Peter R. Wills

Publisher
Wiley (John Wiley & Sons)
Year
1979
Tongue
English
Weight
674 KB
Volume
18
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

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.

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