J. L. P. Benesch

Cryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar

The paper uses cryo-EM to determine the gas-phase structure of β-galactosidase at 2.6 Å resolution, showing structural similarity to its native state.

Single-molecule fluorescence-based approach reveals novel mechanistic insights into small heat shock protein chaperone function

This study uses single-molecule fluorescence to reveal a two-step mechanism by which human Bc (HSPB5) interacts with misfolded proteins to prevent aggregation.

Quantifying protein-protein interactions by molecular counting with mass photometry

This paper demonstrates mass photometry's ability to quantify protein-protein interactions by counting molecules and measuring binding affinities without labels.

Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27

This study investigates how the P182L mutation in HSP27's IxI/V motif disrupts protein interactions, leading to aggregation and disease.

Local unfolding of the HSP27 monomer regulates chaperone activity

This study shows that redox-induced monomerization of HSP27 enhances its chaperone activity but also increases aggregation risk, with mutations in an unstructured region linked to neuropathies.

Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity

This study engineers a polydisperse small heat-shock protein to reveal conserved motifs of oligomer plasticity through structural and functional analysis.

Quantitative mass imaging of single molecules in solution

This paper introduces a method to mass-image single biomolecules in solution with high precision and resolution, enabling the study of molecular interactions and assemblies.