| Sophie Elizabeth Jackson | |
| Birth Place: | Cheshire |
| Workplaces: | University of Cambridge Harvard University |
| Education: | University of Oxford University of Cambridge Imperial College London |
| Thesis Title: | Studies on subtilisin BPN' and chymotrypsin inhibitor 2 |
| Thesis Url: | https://worldcat.org/en/title/556746687 |
| Thesis Year: | 1991 |
| Doctoral Advisor: | Alan Fersht |
| Academic Advisors: | Fraser Armstrong Stuart Schreiber |
Sophie Elizabeth Jackson is a British biochemist and Professor of Chemical Biology at the University of Cambridge. Her research considers protein folding and assembly, She is interested in topological knots, molecular complexes and the β barrel protein.
Jackson was born in Cheshire.[1] She studied mathematics, further mathematics, chemistry and physics at A-Level.[2] She was the first in her family to attend university, and chose to study at The Queen's College, Oxford, because it had the most students from Northern England. At the University of Oxford she worked alongside Fraser Armstrong on electron transfer in metalloproteins.[3] She wanted to move to London, and joined Imperial College London to start a doctorate with Alan Fersht. When he moved to the University of Cambridge, she joined him, and studied the chymotrypsin inhibitor 2 (CI2). In Cambridge Jackson developed the first experimental strategies to monitor protein folding. After earning her doctorate, Jackson joined Harvard University as a postdoctoral fellow with Stuart Schreiber.
Jackson returned to the University of Cambridge as a Royal Society University Research Fellow. Here she established her own research group working on the molecular mechanisms that underpin protein folding/unfolding.[4] [5] [6] Alongside the folding of proteins, Jackson has investigated how proteins form knots. Unfolded, misfolded and unknotted proteins can be toxic.
Unknotted versions of Ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) are implicated in Parkinson's disease. Jackson and her team took different unknotted and knotted versions of UCH-L1 and monitored the refolding. She observed that knots act to slow the protein folding mechanism, creating a complex landscape that permits the formation of intermediate shapes during the folding processes. She also showed that knots in proteins occur close to the sites that enzymes build; indicating they may be important in the lock-and-key shape. She was made a lecturer in 2000 and a professor in 2017.