Measuring the Interaction of Maltose Binding Protein with Maltose Using MicroScale Thermophoresis

25 Apr 2016

This application note investigates the interaction of maltose binding protein (MBP) and its substrate, maltose, drawing upon label-free MicroScale Thermophoresis (MST) as the ideal technique. MST is a powerful technique to study biomolecular interactions in solution. MST makes use of thermophoresis, the phenomenon of molecules migrating in a solution when a temperature gradient is applied. MST showed sensitivity and convenience, whilst being truly label-free experiments in a close-to-native environment. Additionally, MST is not limited by sample viscosity, further proving its versatility.

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ProteomicsProteomics is the systemic bioinformatics study of proteins and amino acids, including their structure, size, function and identification. Tools used in proteomics include chromatography, blotting and gels, protein arrays, mass spectrometry and ELISA and associated analysis software. Analyzers and proteomic systems should be sensitive, high resolution, fast and may be automated for high-throughput.FluorescenceThe emission of fluorescence occurs when a photon of energy is supplied to a fluorescent chemical compound by an external source, causing it to become excited. Fluorescence can be detected and measured for different purposes using microplate readers, fluorescence microscopes, fluorescence scanners, and flow cytometers.Protein BiologyThe analysis of protein expression, identity and function is vital for many areas of life science research and drug discovery. Some of the most commonly used techniques in protein analysis include Western blotting, electrophoresis and mass spectrometry.Label-Free AnalysisMicroscale Thermophoresis
Measuring the Interaction of Maltose Binding Protein with Maltose Using MicroScale Thermophoresis