title: Protein-protein interaction analysis by nuclear magnetic resonance spectroscopy.
abstract: Nuclear magnetic resonance (NMR) is a powerful technique to study protein-protein interactions in solution. Various methods have been developed and applied successfully for locating binding sites on proteins. The application of NMR chemical-shift perturbation to map the protein-protein interfaces is described in this chapter, providing a practical guideline that can be followed to carry out the experiments.
authors.affiliation: Department of Biochemistry and Biophysics, University of North Carolina @ Chapel Hill, Chapel Hill, NC, USA.
authors.forename: Guanghua
authors.initials: G
authors.lastname: Gao
authors.forename: Jason G
authors.initials: JG
authors.lastname: Williams
authors.forename: Sharon L
authors.initials: SL
authors.lastname: Campbell
mesh_terms: D001665:Binding Sites; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D046911:Macromolecular Substances; D011506:Proteins