My research was on protein structure-function relationships. Much of my research was focussed on protein disulphide isomerase (PDI), an enzyme that is responsible for the incorporation of correct disulphide bonds in proteins going through the secretory pathway. I worked on understanding the structure of PDI and how PDI interacts with its client proteins. The client proteins enter the endoplasmic reticulum (ER) in an unfolded state. Once in the ER proteins start to fold and cysteines are oxidised to form disulphide bonds. Often the disulphide bonds formed are not correct and isomerisation to form correct bonds is necessary. Only once the protein is correctly folded will it be allowed to leave the ER and continue along the secretory pathway. Other times the protein is unable to fold and all disulphide bonds must be reduced before the protein can be exported to the cytoplasm for degradation. PDI and other members of the PDI family are responsible for catalysing all three of these processes.
PhD. I got my PH.D from Copenhagen University in Denmark working on the enzymology of plant peroxidases.
I am a member of the Biochemical Society