title: Identifying and studying ubiquitin receptors by NMR.
abstract: Ubiquitin and ubiquitin chains are recognized by a large and growing family of receptor proteins. NMR spectroscopy provides a powerful means to evaluate whether and how a protein binds to ubiquitin. It can be used to measure binding affinities, to map interaction surfaces, and to solve the three-dimensional structure of ubiquitin:receptor complexes. Herein, we describe three NMR techniques of varying complexity that are valuable tools to characterize protein:protein complexes. These include heteronuclear correlation experiments, paramagnetic relaxation enhancement (PRE) experiments via spin labeling, and techniques designed to obtain intermolecular dipole-dipole interactions by nuclear Overhauser effects (NOEs).
authors.affiliation: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA.
authors.forename: Xiang
authors.initials: X
authors.lastname: Chen
authors.forename: Kylie J
authors.initials: KJ
authors.lastname: Walters
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011506:Proteins / Q000737:chemistry; D013113:Spin Labels; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism; D054875:Ubiquitination
chemical_list: D011506:Proteins; D013113:Spin Labels; D025801:Ubiquitin