Sophie E. Jackson

Jackson was born in Cheshire.[1] She studied mathematics, further mathematics, chemistry and physics at A-Level.[1][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.[1] 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.[2][3] When he moved to the University of Cambridge, she joined him, and studied the chymotrypsin inhibitor 2 (CI2).[2] 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.[3]

Jackson returned to the University of Cambridge as a Royal Society University Research Fellow.[1] 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.[1][6]

Unknotted versions of Ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) are implicated in Parkinson's disease.[1] Jackson and her team took different unknotted and knotted versions of UCH-L1 and monitored the refolding.[2][5] 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.[1][5] 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.[1][6]

• Sophie E. Jackson (1 January 1998). "How do small single-domain proteins fold?". Folding & design. 3 (4): R81-91. doi:10.1016/S1359-0278(98)00033-9. ISSN 1359-0278. PMID 9710577. S2CID 1717713. Wikidata Q55067789.
• Sophie E. Jackson; Alan R. Fersht (1 October 1991). "Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition". Biochemistry. 30 (43): 10428–10435. doi:10.1021/BI00107A010. ISSN 0006-2960. PMID 1931967. S2CID 9409985. Wikidata Q34968585.
• Sophie E. Jackson; Marco Moracci; Nadia elMasry; Christopher M. Johnson; Alan R. Fersht (26 October 1993). "Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2". Biochemistry. 32 (42): 11259–69. doi:10.1021/BI00093A001. ISSN 0006-2960. PMID 8218191. Wikidata Q27731428.