Nuclear magnetic resonance (NMR) spectroscopy
NMR spectroscopy is a key tool in structural biology research, allowing for the characterization of protein structures, protein dynamics, and protein-protein interactions. It is advantageous over X-ray crystallography, in that the structures of proteins or peptides in liquid can be solved. Additionally, recent advances in NMR spectroscopy have demonstrated its value in drug discovery, due to its ability to help researchers directly identify ligand binding sites.
The technique involves subjecting a sample to a magnetic field, taking advantage of an intrinsic property of certain atomic nuclei, called spin. In response to the magnetic field, nuclear spins flip from low energy spin states to higher energy states. As the spins flip, energy is absorbed by the nucleus. Absorption spectra data can be used to identify atomic nuclei and the distance between nuclei.
Stable isotopic labeling of peptides allows for the incorporation of NMR active nuclei which can help reduce the complexity of spectra and help scientists obtain new correlations between atoms, for more complete structural information.
Pustovalova Y. et al. (2012) The C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase Η and Rev7 subunit of polymerase Ζ. FEBS Lett. 586: 3051-3056.