Professor Sheena Radford with current biochemistry students
Students in biological sciences can experience first-hand teaching and research from leading academics in the Faculty.
Across the degree programmes students attend lectures delivered by the Faculty’s leading researchers. Professor Sheena Radford recently talked to first year biochemistry students on the intricate world of protein folding.
Sheena is renowned for her work in protein folding and was recently elected into one of the UK's most prestigious medical academies the Academy of Medical Sciences.
Sheena’s work has contributed to an understanding of the mechanisms of protein folding and the importance this has on their appropriate functioning. For example it has been found that the misfolding of proteins is a major influence in ageing. It can also be a contributing factor in the development of disease.
Her lectures are lively and informative and include the use of handsets to allow students to interactively respond to questions in lectures.
Additional subject information is also provided on the virtual learning environment - an online resource of lecture notes, references and podcasts to ensure students get the most up to date experience.
Sheena hopes her research will help inform undergraduate teaching by giving real life examples of research in practice and by encouraging students to develop their understanding both at undergraduate level and beyond. Sheena said: “I hope my lectures will inspire students to think about how their work in the lab and their study of key texts can be developed into real life scenarios. What they learn at undergraduate level will help prepare them for a future career.
“All of our students will get the chance to undertake an independent research project in their final year so it is important they begin to make links between their theoretical study and laboratory experiments and the opportunities to develop this further in a laboratory environment.”
Sheena Radford is Professor of Structural Molecular Biology in the Astbury Centre for Structural Biology.
31st January 2011