The ability to measure and characterize changes in the secondary structure of proteins is critical to many research applications, especially the formulation and development of biotherapeutics. There is direct evidence that changes in secondary structure result in changes in efficacy and specificity. Conventional techniques do not possess the adequate feature set for researchers to See Change™ in their proteins within the required conditions. The need for high sensitivity, a wide dynamic range, a simplified and automated workflow, and high repeatability is signifiant and, until now, has not been adequately provided. The solution for today’s researcher is Microfluidic Modulation Spectroscopy (MMS).
This eBook will introduce you to the novel IR technique called MMS which is designed to address the requirements of today’s development laboratories and fill the characterization gap. This technique is purposely designed to See Change in secondary structure. Data will be presented from measurements of commercially available proteins which demonstrate significant increases in sensitivity, dynamic range, and utility for the characterization of protein secondary structure. It is now possible to measure protein similarity (fingerprinting), quantitation, higher order structure, protein stability, and aggregation through thermal and chemical denaturation methods using a walk-away automated platform. The ability to See Change is enabled by MMS.