Urea and guanidine hydrochloride induced dissociation and denaturation of bacteriophage F2 capsid

International Journal of Peptide and Protein Research
B B Kitchell, R W Henkens

Abstract

A single, low molecular weight protein is found after urea or guanidine hydrochloride (Gdn.HCl) treatment of empty capsids derived from bacteriophage f2. The final product of denaturation is apparently a monomer, existing as a random coil in larger than or equal to 4.0 M Gdn.HCl but in a less extended form in 8.0 M urea. In contrast, an 11 S protein component is isolated after treatment of the intact virus with 4.0 M Gdn.HCl (Zelazo & Haschemeyer, 1969), indicating that RNA plays a role in stabilizing larger subunits. Denaturation by Gdn.HCl occurs in two stages as measured by changes in CD and Stokes radius: dissociation that involves a structural perturbation of aromatic side chains, followed by a major, cooperative transition that evidently results in the loss of all noncovalent structure. Denaturation by urea appears to be a much less cooperative process that occurs in several steps over a wide range of urea concentration (1--7 M). In both urea and Gdn.HCl, dissociation into subunits begins at a lower concentration of denaturant than the major changes in conformation.

References

Sep 1, 1975·Virology·W Paranchych, A K Dunker
Sep 1, 1969·Biochemistry·P O Zelazo, R H Haschemeyer
Jul 17, 1973·Biochemistry·R W Henkens, J L Middlebrook
Jun 19, 1970·Science·P O Zelazo, R H Haschemeyer
Mar 12, 1968·Biochemical and Biophysical Research Communications·R HerrmannU Rudolph
Jul 15, 1960·Biochimica Et Biophysica Acta·W W KIELLEY, W F HARRINGTON

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