One of the most basic and essential characteristics of a biomolecule, such as a protein, peptide, antibody or enzyme, is its structure. From structure, one can assess stability, lot-to-lot reproducibility, and probe differences in activity between batches, formulations, and point mutations of a protein, enzyme, or mAb. Microfluidic Modulation Spectroscopy (MMS) is a powerful technology with the potential to revolutionize bioanalytical research by providing a more accurate and precise means of characterizing proteins than traditional spectroscopic methods.
In this presentation, we’ll delve into the inner workings of MMS and highlight key elements of the technology which differentiate MMS from classic protein secondary structure tools. We’ll share case studies showcasing our ability to provide highly sensitive and repeatable measurements of protein structure, discern between protein products from different vendors and predict those most likely to have the desired activity. We’ll highlight our ability to identify structural and activity changes associated with minor changes in primary sequence. Join us as we unlock the power of MMS and explore the exciting possibilities it holds for the future of protein bioanalytical research.