Student showcase

Bryn Fenwick

Ten years ago, I attended the prestigious London International Youth Science Forum, an outstanding opportunity presented as part of my award for the Science and Technology Prize in New Zealand's 1998 National Science and Technology Fair. The forum included talks by several eminent researchers, as well as visits to selected academic institutions. A visit to Cambridge University was a highlight that, perhaps, started me on my present career.

My research in 1998 was on a pollution trap that I designed in collaboration with the University of Canterbury. The trap could remove rubbish from the waterways around Christchurch. This, however, was not my first science fair project, as I had participated in several regional science fairs and reached the National Fairs in 1993 and 1994. In the first of these my project explored the effects of vitamins on plant growth and their resilience to stress (cold shock). My second successful project surveyed the waste in a local estuary and studied the breakdown of various rubbish types by selected crustaceans. When I finished school I studied physiology and biochemistry, graduating from the University of Canterbury with a first class honours degree in biochemistry, after completing a thesis on an Antarctic fish that lives underneath the sea ice.

After graduating I worked in Professor Juliet Gerrard's biochemistry lab, where I was introduced to protein science. I investigated byssus, the strands that marine mussels use to hold onto rocks. Using new techniques, we separated and characterised the proteins that constitute the strands. I presented the results from this research at a conference in Australia where I was encouraged to apply for a scholarship to further investigate the structures of proteins in Cambridge. I was accepted into Cambridge's Biochemistry PhD programme and was funded by the Cambridge Commonwealth Trusts. I was also accepted to Peterhouse, the oldest college in Cambridge where I received much support during my studies. Additionally, two passed Fellows of Peterhouse were, in 1962, warded the Nobel Prize in chemistry for their studies of the structures of proteins, so I elt very privileged to follow in their footsteps (John Kendrew and Max Perutz).

My research, under supervision, investigated the structure of small G proteins, mutations of which are prevalent in many types of invasive cancers. Working in this stimulating institution, I learned a lot about proteins and the research group introduced me to new protein structure research techniques.

My next step will be a post doctoral fellowship in Barcelona where I will extend the characterisation of the dynamic fluctuations of proteins until I can return to the southern hemisphere. I plan to remain in academia where I hope to foster new ideas and contribute to the advancement of protein science.

To this end, I am interested in finding new ways to examine proteins and their dynamics that relate structure to their biological function.