We investigate the structural dynamics of proteins by NMR spectroscopy to understand the molecular function better. NMR stands for Nuclear Magnetic Resonance Spectroscopy. It reduces effect that the nuclear spins of hydrogen atoms can transition between two energetically different states, and an auto magnetic field.
We can use NMR spectroscopy to study the structural dynamics of intrinsically disordered proteins. These proteins are highly flexible, constantly changing shape, and frequently only fold into a stable structure when they interact with other molecules. We use NMR relaxation experiments to study how the protein backbone moves over very short time scales, ranging from picoseconds to nanoseconds, while focusing on each specific residue along the protein chain.
This protocol will guide you step-by-step through setting up NMR relaxation experiments on an NMR spectrometer aimed at scientists with basic NMR knowledge, it ensures a fast, accurate setup, and introduces key concepts in protein backbone dynamics in an accessible way. This protocol makes NMR relaxation pulse sequences easily accessible to scientists studying protein dynamics. NMR relaxation experiments provide residue specific dynamic insights.
Using this experimental approach, you can better understand backbone dynamics in proteins, the impact of protein-protein interaction on structured dynamics, and structural changes in the response to environmental changes.
