E. James Petersson

This paper demonstrates the directed evolution of a multimodal plastic-degrading enzyme capable of breaking down both polyesters and polyurethane.

This paper develops a method to synthesize thioamide-containing proteins and shows they destabilize β-sheet structures in GB1 and α-synuclein fibrils.

This paper introduces a genetic code expansion method to integrate a fluorophore-quencher pair into proteins for monitoring dynamics, demonstrating applications in studying protein function and drug screening.

This study develops a method to produce highly modified α-synuclein with defined post-translational modifications and a fluorescent label to study their effects on structure and function.

This study uses μMap photo-proximity labeling to compare the interactomes of α-synuclein monomers and fibrils in mouse brain lysate to investigate synucleinopathy mechanisms.

The paper provides methods for site-specific post-translational modification of alpha-synuclein and tau using genetic code expansion and enzymatic approaches, enabling studies of their structural dynamics and aggregation.

This paper introduces hint token learning to improve protein language models on mutational datasets through three case studies, showing better performance than traditional fine-tuning.

The paper uses structural and chemical biology methods to show EX-6 binds selectively to α-synuclein fibrils in MSA tissue, with a 10-fold preference over PD tissue.

This paper designs new bimane-based fluorophores sensitive to polarity and viscosity for imaging α-synuclein in Parkinson's disease.

This study investigates how acetylation of specific lysine sites in α-synuclein affects aggregation and function, identifying K80 acetylation as a potential therapeutic target.

This study investigates how thioamide substitutions in SpyTag affect ligation kinetics with SpyCatcher, showing both faster and slower complex formation depending on substitution position.

The paper determines the structure of the LexA-RecA* complex, revealing a lock-and-key mechanism that triggers SOS response gene induction by enabling LexA cleavage.

This paper expands the working distance of tmFRET to 50 Å using new ligands, enabling precise measurement of conformational changes in maltose binding protein under physiological conditions.

This paper develops a fluorescence method to measure protein conformational dynamics and energetics using time-resolved tmFRET and validates it with EPR spectroscopy.