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(Received for publication, August 15, 1997, and in revised form, September 2, 1997)
From the Department of Pathology, Case Western Reserve University,
Cleveland, Ohio 44106
A recombinant protein corresponding to the human
prion protein domain encompassing residues 90-231 (huPrP(90-231)) was
expressed in Escherichia coli in a soluble form and
purified to homogeneity. Spectroscopic data indicate that the
conformational properties and the folding pathway of huPrP(90-231) are
strongly pH-dependent. Acidic pH induces a dramatic
increase in the exposure of hydrophobic patches on the surface of the
protein. At pH between 7 and 5, the unfolding of hPrP(90-231) in
guanidine hydrochloride occurs as a two-state transition. This
contrasts with the unfolding curves at lower pH values, which indicate
a three-state transition, with the presence of a stable protein folding
intermediate. While the secondary structure of the native
huPrP(90-231) is largely
Volume 272, Number 44,
Issue of October 31, 1997
pp. 27517-27520
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
pH-dependent Stability and Conformation of the
Recombinant Human Prion Protein PrP(90-231)
-helical, the stable intermediate is rich
in 
-sheet structure. These findings have important implications for
understanding the initial events on the pathway toward the conversion
of the normal into the pathological forms of prion protein.
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