Article
Folding and stability of a tryptophan-containing mutant of ubiquitin.
Biochemistry - 13 Jul 1993
Khorasanizadeh S, Peters I D, Butt T R, Roder H
Abstract excerpt
To provide a fluorescence probe for equilibrium and kinetic folding studies on ubiquitin, cassette mutagenesis in an Escherichia coli expression plasmid was used to replace the largely buried Phe 45 by a tryptophan. Under native conditions, the tryptophan fluorescence spectrum of this F45W mutant exhibits a blue-shifted emission maximum at 336 nm indicative of a largely solvent-shielded tryptophan environment. In...
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