mw132 at mole.bio.cam.ac.uk
Fri Aug 10 05:39:19 EST 2001
> From: _Biophysical Chemistry. Part II: Techniques for the Study of Biological
> Structure and Function_ Cantor, CR and Schimmel, PR. WH Freeman & Co. (1980),
> pp. 679-680.
> "... SDS is an effective protein denaturant. It binds to all proteins
> qualitatively the same, at about 1.4 g per gram of amino acid. There is one
> negative charge on each SDS molecule. The resulting charge density due to all
> the SDS in the SDS-protein complex more-or-less overwhelms variations in the
> charges of different protein molecules. ... Charles Tanford and others have
> studied the structure of SDS-protein complexes. Hydrodynamically, they appear to
> be prolate ellipsoids or rods with a constant diameter of about 18 angstroms and
> a length that is linear function of the molecule. ..."
Damn! This means I will have to own up to being wrong to my collegue!
Thanks for the information Nick.
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