Multiple Simultaneous Measurements Provide Improved Characterization of Protein Stability

4 Jan 2018

In this application note, Unchained Labs reveals the importance of using multiple parameters to assess and optimize the stability of proteins. By using the UNit to collect fluorescence spectroscopy and static light scattering data from samples of α-chemotrypsinogen, Unchained Labs illustrates striking differences in the conformational and colloidal stability of formulations, thus demonstrating the need for multiplex analyses.

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Protein CrystallographyProtein crystallization is the process of crystallizing purified proteins for 3D structure analysis by x-ray crystallography. The main methods of protein crystallization include sitting drop, hanging drop and microbatch. It is important to control parameters such as pH, temperature and concentration. Following crystallization, detectors and software are used for data collection and analysis.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.
Multiple Simultaneous Measurements Provide Improved Characterization of Protein Stability