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|NanoTemper Technologies GmbH, Germany|
|ScientificTracks Abstracts: J Proteomics Bioinform|
|Key to understanding the functional role of target proteins is elucidating the structure-function relationship between two proteins or protein complexes. Current analysis is often complex, time-consuming, and lacks data quality. One of the goals of structural biology is to bring together multiple disciplines and methodologies to better characterize proteins and protein complexes. For highly utilized techniques such as cryo-EM, X-ray crystallography and NMR, having the ability to identify and quantify binding affinities as well as analyze conformational and colloidal properties, enables researchers to gain a better understanding of the functional properties of protein targets. During this workshop, you will learn about practical solutions to monitor and optimize protein stability and quality. An overview of the various analytical and biophysical methods commonly used by structural biologist will be discussed. We will share case studies demonstrating the benefits of understanding conformational and colloidal properties of protein complexes and how to use this information for further downstream analysis. Finally, we will share examples of protein-small molecule and protein-protein interactions and novel methodologies that assist researchers in making better decisions.|
Tobias Pfluger studied Chemistry at the Albert Ludwigs University in Freiburg with an emphasis on biochemistry. He received his PhD in Structural Biology investigating the structure and function of membrane proteins involved in cellular signalling cascades. In late 2015, he joined NanoTemper Technologies as an Application Specialist.
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