Uncovering the conformational dynamics of intrinsically disordered proteins on the single molecule level
In this first invited webinar, Prof. Andrea Soranno from the Washington University of St. Louis (Missouri, USA) shared some insights into his work on studying conformational dynamics of IDPs
Intrinsically disordered proteins (IDPs) lack a stable 3D structure; yet they play a key role in many biological functions. Disorder in proteins occurs in many different forms that range from fully disordered proteins and molten globules to linkers and tails flanking folded domains. Quantifying structural heterogeneity and dynamics in disordered proteins is one of the key steps to unveil how the protein sequence encodes for IDP conformations and interactions and, ultimately, function. Join our invited speaker, Dr. Andrea Soranno, to learn how his group uses smFRET and nsFCS to uncover the dynamics and functioning of IDPs, such as the Polypyrimidine Tract Binding Protein, on the single molecule level.
Webinar will be available soon.