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4 ways to help you overcome the limitations of current methods in neurodegenerative disease research

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Monomeric vs. oligomeric Studying small molecule or protein interactions in ND requires working under conditions that either favor the monomeric or oligomeric state of these molecules. Fast conformational dynamics Proteins involved in the onset and progression of neurodegenerative diseases (ND) exist in different conformational states - as monomers or oligomers. Their characterization is very challenging because they can transition from one state to the other very fast. High molecular weight aggregates Misfolded proteins escape cellular quality controls and form aggregates that have the potential to compromise cell function. Because they can have high molecular weight, these aggregates are tricky to work with. Intrinsically disordered proteins Intrinsically disordered proteins (IDP) - those without rigid 3D structures - are associated with many ND. Their structure changes depending on the environment or ligands, which makes is very difficult to work with them. 1 2 3 4 With NanoTemper tools, setup and run times take only a few minutes - so you can work with proteins with fast conformational dynamics with confidence. Many biophysical methods take a long time to set up and run - by the time the measurement is done, your protein may have changed its conformation. Researchers need biophysical methods that allow them to work at low sample concentrations to study the monomeric state, and also at high concentrations to investigate the oligomeric state. NanoTemper offers tools that perform measurements with sample concentrations from mM all the way down to pM. So you can evaluate the monomeric and oligomeric states. Studying IDP with NanoTemper technologies is so easy. You skip immobilization and measure in solution and in close to native conditions. Characterizing IDP with biophysical methods that require immobilization to a solid support and put limitations to the buffer conditions can disturb IDP folding state. Evaluating high molecular weight aggregates with NanoTemper technologies is simple because measurements are independent of the size and mass of the binding partners. In order to understand the modulation of these aggregates by measuring binding affinities, researchers must find technologies that allow them to study high molecular weight aggregates. SOLUTION SOLUTION SOLUTION SOLUTION 4 ways to help you overcome the limitations of current methods in neurodegenerative disease research nanotempertech.com/neurodegenerative-diseases NanoTemper bioanalytical tools empower neurodegenerative disease research CHALLENGE CHALLENGE CHALLENGE CHALLENGE

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