Studying structure evolution of proteins using pulsed dipolar spectroscopy

Abstract

Revealing protein structural evolution is essential for determining its function and interaction with the environment, for understanding disease mechanisms. However, it is challenging for biophysical methods to observe structure evolution, especially at longer distances, limiting their application to few biological systems. Pulsed Dipolar Electron Spin Resonance Spectroscopy (PDS) is powerful method for obtaining such information between the distance ranges of 1 to 10 nm. In PDS, a dipolar signal is acquired from the interaction between a pair of spin labels, from which the distance distribution between them, P(r) may be obtained.