Mass Photometry Analysis of Membrane Proteins in Detergent Micelles.

Analytical Ultracentrifugation for Studying the Oligomeric State and Protein-Protein Interactions of Membrane Transporters.

The protocol for carrying out sedimentation velocity-type analytical ultracentrifugation experiments is presented and developed to help understand the mechanism of multi-component tripartite ATP-independent (TRAP) transporter proteins, which are essential for nutrient uptake in bacteria.

Charge Detection Native Mass Spectrometry for Quantitative Insights into Heterogeneous Protein Interactions.

CD-nMS is established, alone or in combination with SLOMO, as a broadly applicable assay for quantitative characterization of complex biomolecular interactions across soluble, glycosylated, and membrane-associated systems.

Mass photometry and its expanding role in membrane protein research: The Torpedo marmorata nicotinic acetylcholine receptor as case study.

Integral membrane proteins (IMPs) are challenging, yet highly relevant targets for structural biology. Selection of the appropriate membrane mimic environment necessitates extensive optimization using a combination of biochemical and biophysical techniques. We report here on the expanding role of mass photometry (MP) a...

Threading of Single Protein Molecules Through a Solid-State Nanopore.

GFP-Nanobody-Based Fluorescence-Detection Size-Exclusion Chromatography (FSEC) Method for the Expression Screening of Membrane and Secreted Proteins.

Bubble-cell native fluorescence imaging for high-sensitivity label-free protein quantification.

Quantification of low-abundance proteins is critical for biopharmaceutical development, proteomics, and biochemical research; however, existing methods often require trade-offs among sensitivity, sample consumption, and workflow simplicity. Ultraviolet (UV) absorbance at 280 nm remains the most widely used method for r...