Friedrich B M Reinhard

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The thermal stability of proteins can be used to assess ligand binding in living cells. We have generalized this concept by determining the thermal profiles of more than 7000 proteins in human cells by means of mass spectrometry. Monitoring the effects of small-molecule ligands on the profiles delineated more than 50 targets for the kinase inhibitor(More)
We extended thermal proteome profiling to detect transmembrane protein-small molecule interactions in cultured human cells. When we assessed the effects of detergents on ATP-binding profiles, we observed shifts in denaturation temperature for ATP-binding transmembrane proteins. We also observed cellular thermal shifts in pervanadate-induced T cell-receptor(More)
This document demonstrates how to analyze TPP-TR (temperature range) experiments by the NPARC approach. NPARC is a recent extension to the TPP package. It offers a novel methodology to model the temperature dependent melting behavior of each protein, and to detect significant changes in this behaviour due to changes in experimental conditions like drug(More)
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