|Name Sheena Radford|
|Institutions University of Leeds
University of Oxford|
Thesis Domains and conformational flexibility in the catalytic mechanism of the 2-oxo acid dehydrogenase complexes (1987)
Notable awards FRS (2014) FMedSci (2010) Colworth Medal (1996)
Alma mater University of Birmingham, University of Cambridge
Fields Biophysics, Structural biology
Institution University of Leeds, University of Oxford
Folding proteins – from Astbury to Amyloid and Ageing
Sheena Elizabeth Radford FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds.
Radford was educated at the University of Birmingham, the University of Oxford and the University of Cambridge, where she was awarded a PhD in 1987.
Radford's research investigates protein folding, protein aggregation and amyloid disease.
Awards and honours
Radford was elected a Fellow of the Royal Society (FRS) in 2014; her nomination reads:
Sheena Radford is internationally distinguished for her seminal contributions to understanding how the dynamical properties of proteins enable them to fold and function biologically, or to misfold and cause degenerative diseases. She has used sophisticated experimental techniques to characterise protein folding pathways in exquisite detail, in particular demonstrating that non-native as well as native-like interactions can play key roles in stabilising partially folded intermediate states. She has built on these findings to define key steps in the aberrant self-assembly of misfolded proteins into amyloid fibrils, particularly in dialysis related amyloidosis, and to relate these molecular processes to pathogenesis.
Radford was elected a Fellow of the Academy of Medical Sciences (FMedSci) in 2010. Her nomination reads:
Sheena Radford is Professor of Structural Molecular Biology at the University of Leeds. Her achievements have involved the innovative application of biophysical techniques to protein folding problems. Her early work in Oxford on hen lysozyme was the foundation for current views that proteins fold on complex multidimensional landscapes, commonly known as folding funnels. She has extended her research to encompass misfolding and disease and has also developed new physical methods to study ultrafast processes. Sheena's work on dialysis-dependent amyloidosis has shown that protein unfolding of beta-2-microglobulin is a key step in fibril formation.
In 1986, Radford was awarded the Colworth Medal from the Biochemical Society. Radford is a member of Faculty of 1000.