title: Small-Angle Neutron Scattering for Structural Biology of Protein-RNA Complexes.
abstract: This chapter deals with the applications of small-angle neutron scattering (SANS) for the structural study of protein-RNA complexes in solution. After a brief historical introduction, the basic theory and practical requirements (e.g., sample state) for SANS experiments will be treated. Next, model-free parameters, such as the molecular mass and the radius of gyration, which can be obtained without a priori structural information, will be introduced. A more detailed section on the specific properties of SANS (with respect to its sister technique, small-angle X-ray scattering), and their implications on possibilities and limits of model building and interpretation will be discussed with a focus on protein-RNA systems. A practical illustration of the information content of SANS data will be given by applying ab initio modeling to a tRNA-synthetase system of known high-resolution structure. Finally, two present state-of-the-art examples that combine SANS data with complementary structural biology techniques (NMR and crystallography) will be presented and possible future developments and applications will be discussed.
authors.affiliation: Université Grenoble Alpes, Institut de Biologie Structurale, Grenoble Cedex, France; Commisariat à l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Biologie Structurale, Grenoble Cedex, France; Centre National de la Recherche Scientifique, Institut de Biologie Structurale, Grenoble Cedex 9, France; Large Scale Structures Group, Institut Laue-Langevin, Grenoble Cedex, France. Electronic address: frank.gabel@ibs.fr.
authors.forename: Frank
authors.initials: F
authors.lastname: Gabel
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism; D004331:Drosophila melanogaster; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D033363:Neutron Diffraction; D009502:Neutrons; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000378:metabolism; D053838:Scattering, Small Angle; D012996:Solutions; D000072668:Splicing Factor U2AF; D013816:Thermodynamics; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D009687:Nuclear Proteins; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D012996:Solutions; D000072668:Splicing Factor U2AF; C067777:Sxl protein, Drosophila; C000607494:U2AF2 protein, human; C509278:UNR protein, Drosophila; D012313:RNA; C560942:MSL2 protein, human; D044767:Ubiquitin-Protein Ligases; D000604:Amino Acyl-tRNA Synthetases
keywords: Conformational change; Contrast variation; Deuteration; Modeling; Protein; RNA; Scattering length density; Shape; Small-angle neutron scattering