Kyle C. Weber

PFNet calculates residue-level free energy of opening from HX/MS data, enabling scalable and accessible protein stability analysis.

This study resolves a long-standing discrepancy between the structural and functional properties of PFK by showing how activator and inhibitor binding differentially reweights its conformational ensemble.

The paper decodes energetic blueprints of conserved protein folds to explain functional diversity and enables engineered transcription factors with ligand-driven responses.

The paper introduces HXMS, a standardized file format for HX-MS data, and provides PFLink to convert existing data to this format, enhancing data processing and sharing.

MAGPIE aligns many protein complexes on a shared ligand and shows binder residues in interactive 3D, with amino acid frequency graphs and DBSCAN-derived interaction hotspots.