Matthew Gold
Completion date: 2007
Division: Structural Biology
Supervisor: Professor David Barford
Matthew graduated from the ICR with a PhD in 2007 under the supervision of Professor David Barford in the Division of Structural Biology. He is now on an overseas research adventure in Seattle as a Sir Henry Wellcome Postdoctoral Research Fellow. He specialises in the regulation of signalling by scaffold proteins.
Matthew became interested in structural biology during his time as an undergraduate at Cambridge. In his final year, he searched for the best structural biology lab in the UK in which to pursue this interest. "My undergraduate research project advisor recommended the Structural Biology department at the ICR. I was attracted by my supervisor's research, the PhD topic and the unique facilities. Plus, I was impressed by the fantastic quality of research taking place within the other ICR teams."
After a successful application, Matthew went on to investigate a class of signal-organising proteins called A-Kinase Anchoring Proteins (AKAPs): "AKAPs direct the action of protein kinase A (PKA), which is a critical regulator of many biological processes, including cell growth, heart rate and memory formation.
"In the course of my research, I solved the three-dimensional structure of the key PKA-AKAP interface, which establishes the molecular basis for PKA anchoring. I also determined another crystal structure, which revealed that one AKAP (AKAP18) can bind to the small molecule AMP – this was an unexpected clue to its function."
Matthew found his supervisor to be supportive, encouraging and knowledgeable:
"David was brilliant at answering my questions, he allowed me freedom to explore my ideas, and his dedication and enthusiasm for science set an excellent example."
"I used some of my funding to pay for a distance-learning qualification in Protein Crystallography, also to attend conferences and to foster overseas collaborations. One of my lasting memories as an ICR graduate student is stumbling out of the synchrotron facility in Grenoble in the early hours of the morning in pitch darkness under heavy snowfall – we solved the AKAP18 crystal structure on that trip!"
