Robert L. Campbell, Ph.D
- Assistant Professor
- Botterell Hall, Room 644
- Telephone: 613-533-6821
- E-Mail: email@example.com
Faculty BioMy research in collaboration with Dr. Peter Davies' lab has involved the use of X-ray crystallography and molecular modelling to study both the calpain family of enzymes and ice-binding proteins.
Calpains are a family of cysteine proteases that depend on the presence of Ca2+ to allow them to adopt an active conformation. We are studying their structures to try to understand the details of this activation process. We are also using X-ray crystallography and modelling to determine structures of the enyzme in combination with substrates and inhibitors for use in structure-based inhibitor design. Specific inhibitors may be useful in further research studies and as potential lead compounds for the development of pharmaceuticals.
Ice-binding proteins (IBPs) can be divided into two main groups: antifreeze proteins (AFPs) that inhibit ice crystal growth and ice nucleating proteins (INPs) that stimulate ice crystal growth. AFPs bind to the surfaces of ice crystals and inhibit their growth at subzero temperatures, thereby protecting the host organism from freezing damage. We have hypothesized that AFPs bind to ice by first ordering water molecules at the protein's surface to be in an ice-like array. In order to explore this idea, we are using X-ray crystallography combined with homology modelling, molecular dynamics and site-directed mutagenesis to examine the ordering of water molecules around the proteins' surfaces. INPs appear to differ from AFPs predominantly by the size of their ice-binding site. We are attempting to engineer INPs from AFPs and vice versa.
Last Modified: 2017-08-30