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Structural comparison of urease and a GroEL analog from Helicobacter pylori
J W Austin1, P Doig, M Stewart
1Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
Journal of Bacteriology
|November 1, 1992
Abstract:
Electron microscopy of purified protein preparations indicated that Helicobacter pylori urease consisted of circular particles that are 13 nm in diameter, some of which showed indications of threefold rotational symmetry. A GroEL analog of H. pylori (Hp60K) appeared as a disc-shaped molecule with a diameter similar to that of urease but possessed sevenfold rotational symmetry. In a side-view projection, Hp60K appeared as two or four discs stacked side by side.