W. B. Struwe

Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP and its antibody response characterisation

This study determines the 3D structures of TcPOP in open and closed conformations using cryo-EM and evaluates its immunogenicity through antibody responses in mice.

Haptenic adducts of beta-lactam antibiotics elicit antibody responses with narrow clonality and specificity

This study investigates how penicillin G forms immunogenic adducts on proteins and elicits specific antibody responses in mice, revealing clonal dominance and limited cross-reactivity with other beta-lactam antibiotics.

Cooperativity and induced oligomerisation control the interaction of SARS- CoV-2 with its cellular receptor and patient-derived antibodies

The paper investigates how multivalent interactions between SARS-CoV-2 spike protein, ACE2 receptor, and patient-derived antibodies influence viral entry and antibody inhibition.

Analysis of SARS-CoV-2 spike glycosylation reveals shedding of a vaccine candidate

The paper compares glycosylation patterns between SARS-CoV-2 viral spikes and a vaccine candidate, showing differences in secretion pathways and potential implications for immune response and vaccine design.

Single molecule mass photometry of nucleic acids

This paper demonstrates that mass photometry can detect and quantify nucleic acids with high accuracy and speed, using sub-picomole samples.

Hyper-Truncated Glycans Augment the Activity of Neutrophil Granule Myeloperoxidase

This study identifies hyper-truncated glycans on neutrophil myeloperoxidase (MPO) that enhance enzyme activity and inhibition potential, revealing their functional role in immune responses.

Correlating glycoforms of DC-SIGN with stability using a combination of enzymatic digestion and ion mobility MS

This study uses mass spectrometry to show that the stability of DC-SIGN is better correlated with the number of glycosylation sites than with glycan mass or length.

Mass Photometry of Membrane Proteins

This study uses mass photometry to analyze membrane proteins and mimetic systems, revealing structural insights and improving nanodisc assembly characterization.

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.

Quantifying the heterogeneity of macromolecular machines by mass photometry

This paper demonstrates that mass photometry accurately quantifies sample heterogeneity with high resolution and minimal volume, outperforming negative stain electron microscopy in detecting proteasome assemblies.

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.