The calcitonin peptide (Ct) family includes intrinsically disordered peptides which function as hormones (regulating glucose levels in the blood, calcium resorption in the bone, vasodilation and the transmission of pain signals, and triggering migraine attacks). They have highly conserved sequence elements, share key structural features, and bind to similar receptors. Some Ct sequences are associated with amyloid diseases and aggregate into pathological fibers.  We use a nanosecond laser-pump spectroscopy technique to measure end-to-end distances and rates of contact formation in these IDPs. We will discuss our recent results on the effect of electrostatic interactions on both their structure and dynamics. We find that electrostatic interactions can dramatically affect the roughness of IDP energy landscape, and therefore their rate of conformational sampling. This is a key parameter which allows IDPs to function.

Internal dynamics and chain expansion: the role of electrostatics in amyloid versus non-amyloid IDPs of the Ct family

252nd National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.