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Nature Macmillan Publishers Ltd 1998 Unfolded conformations of
 

Summary: Nature © Macmillan Publishers Ltd 1998
8
Unfolded conformations of
-lytic protease are more
stable than its native state
Julie L. Sohl*, Sheila S. Jaswal§ & David A. Agard*§
* Graduate Group in Biophysics and the Howard Hughes Medical Institute,
§ Department of Biochemistry and Biophysics, University of California at
San Francisco, San Francisco, California 94143-0448, USA
These authors contributed equally to this work
Present address: Department of Molecular and Cell Biology,
University of California at Berkeley, Berkeley, California 94720, USA.
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-Lytic protease ( LP), an extracellular bacterial protease, is
synthesized with a large amino-terminal pro-region that is essen-
tial for its folding in vivo and in vitro1,2
. In the absence of the pro-
region, the protease folds to an inactive, partially folded state,
designated `I'. The pro-region catalyses protease folding by
directly stabilizing the folding transition state ( 26 kcal mol-1

  

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

 

Collections: Biotechnology; Biology and Medicine