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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
212:. Here she established her own research group working on the molecular mechanisms that underpin protein folding/unfolding. Alongside the folding of proteins, Jackson has investigated how proteins form knots. Unfolded, misfolded and unknotted proteins can be toxic.
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188:(CI2). In Cambridge Jackson developed the first experimental strategies to monitor protein folding. After earning her doctorate, Jackson joined
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136:. Her research considers protein folding and assembly, She is interested in topological knots, molecular complexes and the
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367:(26 October 1993). "Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2".
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they may be important in the lock-and-key shape. She was made a lecturer in 2000 and a professor in 2017.
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305:(1 October 1991). "Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition".
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on electron transfer in metalloproteins. She wanted to move to
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Studies on subtilisin BPN' and chymotrypsin inhibitor 2
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557:"The Mystery of Knotted Proteins"
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180:. When he moved to the
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415:References
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160:. At the
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