New NMR Tools for Studying Difficult Proteins and Protein- Ligand Interactions
Sprache des Titels:
Using NMR to determine the structure and/or ligand interactions of proteins, ultimately requires an assignment of protein atoms to observed NMR resonances. Structural information is often extracted in the form of distances between atoms derived from NOEs.
For large proteins, this approach becomes increasingly difficult, because the increased amount of signals leads to larger signal overlap.
Selective labelling techniques address this issue in various ways: selective isotopic labelling strategies can greatly simplify resonance assignment and protein-ligand binding studies. Selective labelling also allows the introduction of exogenous groups with particular NMR properties, such as paramagnetic centers, so-called spin labels, into proteins at defined positions. Paramagnetic relaxation enhancements can then be used to study protein-membrane interactions, protein dynamics, and the visualization of lowly populated states and interactions.