title: Overview on the use of NMR to examine protein structure.
abstract: Any protein structure determination process contains several steps, starting from obtaining a suitable sample, then moving on to acquiring data and spectral assignment, and lastly to the final steps of structure determination and validation. This unit describes all of these steps, starting with the basic physical principles behind NMR and some of the most commonly measured and observed phenomena such as chemical shift, scalar and residual coupling, and the nuclear Overhauser effect. Then, in somewhat more detail, the process of spectral assignment and structure elucidation is explained. Furthermore, the use of NMR to study protein-ligand interaction, protein dynamics, or protein folding is described.
authors.affiliation: Protein Biophysics, Institute for Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
authors.forename: Vincent
authors.initials: V
authors.lastname: Breukels
authors.forename: Albert
authors.initials: A
authors.lastname: Konijnenberg
authors.forename: Sanne M
authors.initials: SM
authors.lastname: Nabuurs
authors.forename: Jurgen F
authors.initials: JF
authors.lastname: Doreleijers
authors.forename: Nadezda V
authors.initials: NV
authors.lastname: Kovalevskaya
authors.forename: Geerten W
authors.initials: GW
authors.lastname: Vuister
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000295:instrumentation / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011506:Proteins