Some of the Techniques We Use

• Genetic engineering - to produce modified forms of bovine pancreatic trypsin inhibitor and trypsin.
  
  
• Kinetic analysis - to establish folding mechanisms, and to measure the energetic consequences of mutations.
  
  
• NMR spectroscopy - to study internal dynamics of BPTI variants.
  
  
• High performance liquid chromatography (HPLC) - to purify proteins and peptides, to separate disulfide-bonded folding intermediates, and for peptide mapping to identify disulfide bonds.
  
  
• Non-denaturing gel electrophoresis - to separate disulfide bonded folding intermediates for kinetic analysis.
  
  
• Titration calorimetry - to analyze the thermodynamics of the interaction between BPTI and trypsin.
  
  
• Urea gradient gel electrophoresis - to sudy denaturant induced unfolding. We don't actually do very much of this, but David Goldenberg has written reviews and book chapters about how to do it, and we have a web page that provides some basic information.