Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits
 

Summary: The folding landscape of Streptomyces griseus
protease B reveals the energetic costs and benefits
associated with evolving kinetic stability
STEPHANIE M.E. TRUHLAR,1
ERIN L. CUNNINGHAM,2
AND DAVID A. AGARD1,2,3
1
Graduate Program in Chemistry and Chemical Biology, 2
Graduate Group in Biophysics, and 3
Howard Hughes
Medical Institute and the Department of Biochemistry and Biophysics, University of California, San Francisco,
San Francisco, California, 94143-2240, USA
(RECEIVED July 28, 2003; FINAL REVISION October 15, 2003; ACCEPTED October 16, 2003)
Abstract
Like most extracellular bacterial proteases, Streptomyces griseus protease B (SGPB) and -lytic protease
( LP) are synthesized with covalently attached pro regions necessary for their folding. In this article, we
characterize the folding free energy landscape of SGPB and compare it to the folding landscapes of LP and
trypsin, a mammalian homolog that folds independently of its zymogen peptide. In contrast to the thermo-
dynamically stable native state of trypsin, SGPB and LP fold to native states that are thermodynamically
marginally stable or unstable, respectively. Instead, their apparent stability arises kinetically, from unfolding

  

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

 

Collections: Biotechnology; Biology and Medicine