Katrine Wallis

Katrine Wallis is a researcher at Coventry University, where she continues her work on the structure and function of mammalian protein disulphide isomerases (PDIs). She previously held research positions at the University of Warwick and Oxford University, contributing to key advances in understanding disulphide bond formation and PDI dynamics. Her research bridges biochemistry, structural biology, and molecular biophysics.

Her research focuses on the mechanistic and structural aspects of PDIs, particularly human PDI and related proteins like ERp27 and P5. She investigates how disulphide bonds are incorporated during protein folding, the conformational dynamics of PDI domains, and the functional implications of inter-domain flexibility. A major interest is the role of the x-linker region in modulating substrate access and enzyme plasticity.

The published articles highlight a consistent focus on the structural dynamics of PDIs using techniques such as NMR and biochemical characterization. Themes include domain mobility, substrate binding mechanisms, dimerization, and conformational regulation—indicating a deep commitment to understanding the molecular basis of PDI function in cellular redox environments.

Katrine Wallis has collaborated extensively with leading researchers such as R.B. Freedman, L.W. Ruddock, and R.A. Williamson. While no formal advising or grant information is provided, her independent research agenda and publication record suggest active mentorship and funding involvement.

Her work contributes to the broader understanding of protein quality control in the endoplasmic reticulum, with implications for diseases involving oxidative stress and misfolded proteins. She is also developing new, more robust assays for measuring PDI activity, aiming to overcome limitations of current methods.