TECHNICAL NOTE
Quick protein binding analysis by label-free thermal shift
analysis on the Tycho NT.6
Mariam Mohamadi, Nuška Tschammer and Dennis Breitsprecher
NanoTemper Technologies GmbH, Floessergasse 4, 81369 Munich
Introduction
The lock-and-key model first postulated by the famous chemist Emil Fischer
proposes that enzymes and their substrates must fit together like locks and keys in
order to fulfill their physiological functions. Even though it has long become clear
that biological systems are nowhere near as rigid as their metallic namesakes, the
principle of molecules interacting together three-dimensionally is the basis for
almost all biological processes. Of course this is not only true for enzymes, but for all
types of protein interactions. Only a protein that is correctly folded and structurally
intact can do its job properly. For researchers working with proteins, it is therefore
fundamentally important to be able to analyze both protein structure and function.
The Tycho™ NT.6 system offers a rapid,
simple and straightforward way to
check protein functionality and, as a
consequence, its quality.
To determine whether a protein is functional and able to bind its interaction
partner or ligand, Tycho NT.6 can examine protein-ligand interactions by
performing a label-free thermal shi analysis. Suitable ligands can be varied and
diverse, ranging from ions, sugars and small molecules to nucleotides and lipids.
By recording and comparing highly precise unfolding profiles, ligand-induced
