title: Protein-protein interaction analysis by nuclear magnetic resonance spectroscopy.
abstract: Nuclear magnetic resonance (NMR) has continued to evolve as a powerful method, with an increase in the number of pulse sequences and techniques available to study protein-protein interactions. In this chapter, a straightforward method to map a protein-protein interface and design a structural model is described, using chemical shift perturbation, paramagnetic relaxation enhancement, and data-driven docking.
authors: Department of Biochemistry and Biophysics, University of North Carolina, 120 Mason Farm Road, CB # 7260, 3100A-C Genetic Medicine, Chapel Hill, NC, 27599, USA.
authors: Peter M
authors: PM
authors: Thompson
authors: Moriah R
authors: MR
authors: Beck
authors: Sharon L
authors: SL
authors: Campbell
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D062105:Molecular Docking Simulation; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins