Dds. Smith et al., GREEK KEY JELLYROLL PROTEIN MOTIF DESIGN - EXPRESSION AND CHARACTERIZATION OF A FIRST-GENERATION MOLECULE, Protein engineering, 8(1), 1995, pp. 13-20
A protein designed de novo to fold into the Greek key jellyroll struct
ural motif has been studied. Theoretical analyses have indicated that
the designed sequence should adopt the beta-strand arrangement of the
Creek key jellyroll rather than any other arrangement. A synthetic gen
e was constructed and the protein expressed in Escherichia coli. Circu
lar dichroism spectroscopy is consistent with the protein folding into
the designed conformation and also suggests the presence of tertiary
structure, Fluorescence spectroscopy showed the single tryptophan to b
e partially buried, while denaturation studies showed changes in fluor
escence to precede alterations in secondary structure.