Microfluidic modulation spectroscopy (MMS) analysis combines laser spectroscopy, microfluidics, and signal processing to probe protein backbones directly using mid-infrared light. In this way, MMS provides direct, label free measurements, giving researchers information on higher order structure, aggregate formation, protein stability, and concentration.
With MMS, proteins can be measured over a broad concentration range (0.1 mg/mL to over 200 mg/mL for secondary structure measurements, and from 0.01 mg/mL to 200 mg/mL for protein quantitation) with relative ease in a variety of environments without the issues of background fluorescence and light scattering, or complications related to protein size.
Download this white paper from RedShiftBio to learn about:
- How MMS works
- Using MMS analysis to calculate higher order protein structures
- Monitoring and understanding the mechanisms of protein stability and aggregation with MMS measurements
- MMS-enabled derivation of protein similarity and quantitation
