Sheena E. Radford

Biosketch

Sheena Radford is Astbury Professor of Biophysics and Royal Society Research Professor at the University of Leeds, UK. Born in Altrincham, UK, she obtained a BSc in Biochemistry at the University of Birmingham, UK, in 1984 and PhD at the University of Cambridge, UK, in 1987. After completing a Royal Society University Research Fellowship at the University of Oxford she became lecturer at the University of Leeds in 1995. She was an inaugural member of the Astbury Centre for Structural Molecular Biology and was its Director from 2012-2021.
Radford has been awarded the UK Biochemical Society Colworth Medal, the Royal Society of Chemistry Astra Zeneca prize and Rita and John Cornforth Award, the Hites Award of the American Society for Mass Spectrometry, the Protein Society Carl Brändén award and the UK Biochemistry Society Centenary Award for 2025. She is a Fellow of the Royal Society of Chemistry, the Royal Society of Biology, the European Molecular Biology Organisation (EMBO), the Academia Europaea, the Academy of Medical Sciences and the Royal Society. She is Doctor honoris causa from the University of Liège, and was made Officer of the Most Excellent Order of the British Empire (OBE) for services to molecular biology.

Research Interests

Sheena Radford’s research is multidisciplinary in nature, spanning structural molecular biology, protein biochemistry and biophysical analyses, and linking these approaches with cell biology and assays in cells and tissues. Her major expertise is in the measurement of the conformational dynamics of proteins and the elucidation of the role that these motions play in protein folding and misfolding. Understanding the fundamental mechanisms by which proteins misfold and self-assemble into amyloid fibrils that contribute to diseases spanning Alzheimer’s, Parkinson’s and type 2 diabetes is one research focus. Her laboratory has used and developed biophysical methods to decipher the nature of the early protein-protein interactions that commit proteins to aggregate into amyloid and to show how amyloid fibrils form and structurally change with time. Deciphering how outer membrane proteins (OMPs) fold and insert into the outer membranes of Gram-negative bacteria, facilitated by molecular chaperones and catalysed by the beta-barrel assembly machinery (BAM), is a second major area of research. Combining biophysical methods with NMR and cryoEM, her lab has shown how SurA and Skp chaperone their OMP clients, and how SurA delivers OMPs for vectorial folding on BAM. She also works closely with the biopharmaceutical industry in developing proteins to be more resilient to the stresses of bioprocessing.