Oxidative folding of proteins
Formation of disulfide bonds between cysteine residues is an important post-translational modification. Our research focuses on how disulfide bond formation is catalyzed, how mis-oxidized proteins are isomerized back to their native correctly folded state, and on the development of novel protein expression strains. We investigate these principles in vivo using genetic selections and synthetic biology in the model organism E. coli.
Recent project aims:
a) Understand the mechanisms of oxidative protein folding and the diversity of enzymes involved in this process
b) Identify novel enzymes which can assist in the oxidative folding of proteins
c) Use our discoveries to engineer E. coli strains that can express high yields of multi-disulfide bonded proteins
Merging the power of E. coli genetics with antibody applications.
Work from the Berkmen lab has resulted in the creation of bacterial strains capable of expressing full-size mammalian IgG antibodies, allowing production, selection and engineering of these uniquely mammalian molecules in a microbial system.