Rate My Professor Sheena Radford

Radford's research investigates protein folding and misfolding mechanisms, focusing on amyloid assembly in diseases including Alzheimer’s, Parkinson’s, type II diabetes, and dialysis-related amyloidosis, outer membrane protein folding in Gram-negative bacteria, and stabilization of biopharmaceuticals against aggregation. Her group integrates biophysical techniques such as NMR, mass spectrometry, cryo-EM, and single-molecule approaches to study conformational dynamics and self-assembly. With over 360 peer-reviewed publications exceeding 39,000 citations, key works include “Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis” (Nature, 1997), “A new era for understanding amyloid structures and disease” (Nature Reviews Molecular Cell Biology, 2018), and “Structural evolution of fibril polymorphs during amyloid assembly” (Cell, 2023). Her impact is recognized by awards including the OBE (2020), election as Fellow of the Royal Society (2014), Academy of Medical Sciences Fellow (2010), National Academy of Sciences international member (2024), and Biochemical Society Centenary Award (2025). She serves as Associate Editor of the Journal of Molecular Biology, Trustee of the UK Dementia Research Institute, and has given over 475 invited lectures internationally.