If you study neurodegenerative diseases (ND), you already know they are one of the most challenging — and fascinating — types of diseases to study.
With protein aggregation being a hallmark of ND, NanoTemper’s Senior Application Specialist, Dr. Andreas Langer, met with SelectScience to discuss how intrinsically disordered proteins (IDPs) are at the heart of the challenge for scientists. Check out the article here.
The big takeaway from that conversation was identifying why IDPs are tricky to characterize and what’s the best biophysical method to do that.
Why IDPs are tricky to characterize
IDPs are like busy toddlers that are continuously moving from one toy to another — IDPs don’t hold one conformation long and they can quickly and continuously aggregate and bind co-factors and ligands. Like asking a toddler to stop and pose for a photo that accurately and comprehensively represents their personality and interests, you can’t hold IDPs in place (i.e. immobilize them to a solid substrate) and expect to get a realistic picture of their interactions with other molecules.
The best way to characterize IDPs
Fear not, brave scientist. You can study an IDP (or any protein) without the need to immobilize it first. NanoTemper’s technologies use in-solution measurements that allow for the inherent flexibility of IDP conformation and interactions with small or large molecules. Learn how NanoTemper’s technologies help you overcome this neurodegenerative disease research challenge here.
