The 2016 Centenary Award was presented to Patrick Cramer from Max Planck Institute for Biophysical Chemistry, Germany.  The award is made in recognition of Patrick’s successful systems biology approach to uncovering the importance of and mechanisms in transcriptome surveillance and RNA degradation in the balanced production of mRNAs.  Furthermore, two important crystal structures were published in 2013.

Patrick Cramer received his award at the 80th Harden Conference: Machines on Genes IV – Mechanisms of Actions of Large Macromolecular Machines on Genes Across Biological Scales at Shrigley Hall Hotel, Macclesfield, UK, 31 July—4 August 2016.

Read his review article published in Biochemical Society Transactions here: Structure determination of transient transcription complexes. 

The 2013 Centenary Award was presented to G. Marius Clore. 

Read his article 'Seeing the invisible by paramagnetic and diamagnetic NMR' published in Biochemical Society Transactions here. 

The 2012 Centenary Award was presented to David Baker.

Read his article 'Protein folding, structure prediction and design' published in Biochemical Society Transactions here.

The 2011 Centenary Award was presented to Nahum Sonenberg.

Read his review article 'Signalling to eIF4E in cancer' published in Biochemical Society Transactions here. 

The Centenary Award will be presented to Professor Gideon Davies in 2024. Gideon obtained his PhD from the University of Bristol in 1990 before moving to the EMBL Hamburg. He moved to York, with visits to Grenoble and Uppsala before taking up a Royal Society University Research Fellowship (URF) in 1996. In 2000, he was the inaugural “Peter Wall Catalytic Visitor” at the University of British Columbia before being made a full Professor of the University of York in 2001. In 2016, he received the Royal Society "Ken Murray" Research Professorship. His research work spans chemistry and biology with a focus on the enzymes that synthesise and degrade carbohydrates and glycans. He is well known for his work on enzyme mechanism, following the unusual contortions of sugars in enzyme active sites, and building on this to develop inhibitors and more recently activity-based probes. Recent impact includes the development of inhibitor classes that underpinned the development of compounds in clinical trial for neurodegeneration, studies of the human heparanase enzyme and development of new anti-cancer compounds as well as applying activity probes and new chemistries in the field of industrial biomass conversion.

On winning the Centenary Award for 2024, Gideon said “It is especially important to me that this award, beyond research impact, also reflects a commitment to nurture talent within the scientific community. I am so proud of the wonderful, diverse, group of young and early-career scientists I have worked with throughout my career and to see them thriving in academia, industry, education and child support is the true highlight of my career. I hope the award will inspire other young scientists, from all backgrounds, to dive into the exciting world of the glycosciences.”

Gideon presented his Award lecture at Advances and New Horizons in Glycobiology on 5 December 2024.

Read Gideon's review article published in the Biochemical Journal - Activity-based probes for dynamic characterisation of polysaccharide-degrading enzymes

The Centenary Award will be presented to Professor Sheena Radford OBE in 2025. Sheena obtained her BSc in Biochemistry from the University of Birmingham in 1984 and PhD from the University of Cambridge in 1987, before moving to the University of Oxford, where she was first a postdoc and then Royal Society University Research Fellow in the Oxford Centre for Molecular Sciences. In 1995, she moved to the University of Leeds as Lecturer in Biochemistry and was a founder member of the Astbury Centre for Structural Molecular Biology. She was made a full Professor of the University of Leeds in 2000 and was Director of the Astbury Centre from 2012-2021. She currently holds the position of Royal Society Research Professor and is the Astbury Professor of Biophysics. Her research spans the disciplines, focussing on the question of how proteins fold, how gram-negative bacteria fold proteins into the outer membrane to create their cell wall, and how proteins misfold and form amyloid in disease. She has received several awards in recognition of her work, including the Biochemical Society’s Colworth Medal, Membership of EMBO and of the Academia Europaea, Fellowships of the Royal Society, Academy of Medical Sciences, Society of Biology and Royal Society of Chemistry and was made member of the Order of the British Empire (OBE) in 2020 for her services to molecular biology.

Sheena said: "I am delighted and humbled to receive this award. I have been a member of the Biochemical Society since I was an undergraduate, which makes the award even more special for me. I have been lucky to have worked with a fantastic group of talented early career scientists and collaborators both in the Astbury Centre at Leeds and across the globe. I thank them all. The very best of science is performed in collaborative and supportive teams. If I have helped to promote that working ethos, and to help others, then I have done my job! The field of protein folding has never been more exciting and I hope that this award will inspire others to join our community and help to tackle the dire consequences caused when protein folding goes wrong.”

Sheena presented her Award Lecture at Protein Evolution, Design and Bioinformatics Edinburgh on 15 May 2026.

The 2014 Centenary Award was presented to Professor Susan Taylor from the Howard Hughes Medical Institute, University of California San Diego, USA. Susan has made fundamental and pioneering contributions to understanding the structure and function of protein kinases. Susan received her undergraduate degree at the University of Wisconsin and her PhD in Physiological Chemistry from the Johns Hopkins University. She did her postdoctoral work at the MRC Laboratory of Molecular
Biology in Cambridge with Brian Hartley and then went to the newly founded University of San Diego, first as a postdoctoral fellow with Nathan Kaplan and then rising through the ranks to the level of Distinguished Professor of Chemistry and Biochemistry and of Pharmacology. She is also a Howard Hughes Medical Institute Investigator.

Her research on the structure and function of cAMP-dependent protein kinase (PKA) led to her solving the crystal structure of the first protein kinase in 1991. The PKA catalytic subunit has served as the prototype for the entire protein kinase superfamily that regulates so many biological processes. Her subsequent structures of the PKA regulatory subunits and most recently of full-length tetrameric holoenzymes show how a large macromolecular signalling complex is assembled at specific sites in the cell.