Athene Donald

Dame Athene Margaret Donald DBE FRS HonFInstP HonFRSC (née Griffith; born 15 May 1953) is a British physicist. She was Professor Emerita of Experimental Physics at the University of Cambridge, and former Master of Churchill College, Cambridge.

Donald was born Athene Margaret Griffith in London, to Walter Griffith and Annette Marian Tylor. She was educated at Camden School for Girls and the University of Cambridge where she was an undergraduate student of Girton College, Cambridge. She earned a bachelor's degree in Natural Science (Theoretical Physics), followed by a PhD in 1977 for research on electron microscopy of grain boundary embrittled systems.

Donald worked at Cornell University as a postdoctoral associate, where she switched from working on metals to polymers, before returning to Cambridge (Department of Materials Science) in 1981 and to the Cavendish Laboratory in 1983. She became Professor of Experimental Physics in 1998. Her major domain of study is soft matter physics, particularly its applications to living organisms and the relationship between structure and other properties.

Her research has applied microscopy, and in particular environmental scanning electron microscopy, to the study of both synthetic and biological systems, notably protein aggregation.

Further details of her research can be found in the citation for the Faraday Medal she was awarded by the Institute of Physics in 2010:

Professor Donald's deeply innovative and productive research is in experimental soft condensed matter physics, incorporating polymer and colloidal physics, and more recently biological physics. Her early Cornell work on glassy polymer crazing remains very influential and was followed by insightful studies of shear deformation in liquid crystal polymers (LCPs).

Here she was able to demonstrate the ubiquity of the so-called banded texture after shear of LCP's and study the underlying packing of the molecules by electron microscopy showing how they followed a serpentine trajectory in several thermotropics. She also carried out important work on lyotropic systems, including a synthetic polypeptide, studying its gelation and phase diagram.

Donald's mid-career launch into biological physics followed naturally from this polymer work leading to the physics of food and thence to starch. The starch granule structure and its changes during different processing histories were brilliantly analysed using a novel X-ray scattering technique. Structural changes during cooking, with the amylopectin molecule imaginatively treated as a side chain liquid crystalline polymer, brought understanding to different processing treatments. The misfolding of proteins forming amyloid fibrils is well recognized in the aetiology of many diseases, particularly those of old age. Donald's recent work has demonstrated that this important and challenging problem can be powerfully addressed by the approaches of polymer science and furthermore suggests an intriguing connection between the structures observed in both fields.