Mechanisms of Helicases and RNA Chaperones by NMR
A protein with RNA chaperone activity binds transiently and non-specifically to RNA. Consequently, it disrupts RNA-RNA interactions and leads to a loosening of RNA structures. Chaperones do not need external energy. This is in contrast to helicases that also resolve RNA structures but require energy in the form of ATP for their function.
Our research goal is to investigate both chaperones and helicase and to elucidate their molecular mechanisms of action. We aim at understanding what are the contributions that lead to a -partial- destabilization of structural element in the RNA and how this leads to changes in their conformational dynamics. Therefore, we employ modern NMR spectroscopic techniques and time-resolved NMR in conjunction with photo-caged RNAs.
RNA folding & NMR
Refolding of stable RNA conformations play an important role in various fundamental biological processes such as transcription and translation. This is particularly highlighted by riboswitches that regulate these processes in bacteria. As the transition between the conformational states occurs on the seconds timescale time resolved NMR spectroscopy is a well suited tool to investigate such dynamics with atomic Resolution. In this Research Field we aim at (i) expanding our experimental tool box for time resolved NMR with respect to sensitivity, temporal resolution and applicability and (ii) exploring new molecular probes (e.g. hetero nuclei such as 13C, 15N and 19F) to expand our abilities to describe dynamics of RNAs.