Local interactions and transient secondary structures govern backbone dynamics of intrinsically disordered proteins

Abstract

The lack of well-defined structures in intrinsically disordered proteins (IDPs) calls for a fundamental reassessment how their amino-acid sequences codes for functions. Some attention has been paid to nascent structures, but a missing link is sequence-dependent backbone dynamics. In our previous study, we showed that sequence-dependent backbone dynamics in the N-terminal disordered region of ChiZ arises from the formation of correlated segments stabilized by polyproline II (PPII) propensities and salt bridges.