Speaker
Description
Nuclear Magnetic Resonance (NMR) spectroscopy is an enabling technology capable to provide information and answers to biological problems that cannot be obtained by other means. NMR studies, both in solution and in the solid-state, can inform on the structure of a macromolecule in many different environments ranging from buffered solutions to intact cells, can provide insight into dynamic processes, and allow to monitor biomolecular interactions that are key to the cellular response to environmental, developmental and growth signals.
NMR is central to the study of folding, unfolding and disordered states of proteins because of its capability to define the structures of proteins in solution and to characterize the dynamic properties that are inherent to function.
As such, we will provide some examples of recent applications of NMR spectroscopy carried out at the CERM/CIRMMP infrastructure, the Italian centre for NMR spectroscopy of Instruct-ERIC.
