Joan‐Emma Shea

A water-pinning hotspot drives templated tau aggregation

In a minimal tau fibril model, residue 300/301 binds incoming peptide first and carries the most release-prone hydration water. Spin-labelling site 300 impairs locking and suppresses seeded growth.

Reconstructing time-resolved inter-residue distance distributions in a protein ensemble during functional dynamics in solution

This paper develops a method to reconstruct time-resolved inter-residue distance distributions in proteins during functional dynamics using rs-TiGGER spectra and applies it to AsLOV2.

Context-Aware Hydrophobicity Modeling: HydroMap and FastHydroMap

This paper introduces HydroMap and FastHydroMap models to predict hydrophobicity from water features, enabling rapid and accurate computation of dewetting free energy for proteins and surfaces.

BAG2 Condensates Couple Proteostasis to CD8+T Cell Surveillance

This paper identifies I-PDBs as BAG2-driven organelles that link proteostasis to CD8+ T cell surveillance by processing pathological tau into antigenic peptides.

Hydraulic Activation of the AsLOV2 Photoreceptor

This study shows blue light or high pressure activates AsLOV2 by expelling structured water, causing conformational changes and suggesting hydration water drives protein mechanics.

Precision Proteoform Design for 4R Tau Isoform Selective Templated Aggregation

The paper designs a 19-residue peptide that selectively induces aggregation of 4R tau over 3R tau, revealing structural and amino acid determinants of tauopathy propagation.

Discovering pathways through ribozyme fitness landscapes using information theoretic quantification of epistasis

The paper uses information theory to model epistasis in ribozymes, predicting high-activity mutants that were validated experimentally and revealed an evolutionary bridge between ribozyme families.

The Proline-rich Domain Promotes Tau Liquid Liquid Phase Separation in Cells

The paper identifies the proline-rich domain (PRD) of tau as a driver of liquid-liquid phase separation (LLPS) in cells, showing its phosphorylation-dependent behavior and interaction with microtubules.