Register for free to
view the full innovation profile.
New ESI source design strategies that prevent heat loss, protein degradation, and acidification of protein solution.
About
Technology This technology provides a temperature-controlled electrospray ionization (ESI) source that allows for highly precise and accurate characterization of the thermal stability and aggregation of proteins by ESI mass spectrometry (MS). The ESI source was designed to eliminate artifacts that interfere with the detection of temperature-induced changes of biopolymer properties. It minimizes biopolymer degradation prior to the analysis, and incorporates a long heat shield to greatly improve thermal control during sample introduction into the ESI interface. This technology, coupled with high specificity of MS detection, enables the study of both reversible and irreversible processes of biopolymers in solution, and allows the early stages of heat-induced protein aggregation to be characterized in detail by monitoring both conformational changes and formation of oligomeric complexes as a function of temperature. Advantages New ESI source design strategies that prevent heat loss, protein degradation, and acidification of protein solution Adjustable sample flow rate allows process triggered by heat stress to be monitored in a time-resolved fashion Highly precise and accurate characterization of protein unfolding and aggregation Applications Reversible unfolding of proteins Irreversible unfolding and aggregation of proteins Kinetic measurements of protein aggregation AVAILABILITY: Available for Licensing or Sponsored Research DOCKET: UMA 10-39 PATENT STATUS: Patent issued US 8,766,179