An efficient protocol for NMR-spectroscopy-based structure determination of protein complexes in solution.
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Michael Nilges | Michael Sattler | Cameron D Mackereth | Tobias Madl | M. Nilges | B. Simon | T. Madl | M. Sattler | Cameron D. Mackereth | Bernd Simon
[1] M Nilges,et al. A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints , 2008, Journal of biomolecular NMR.
[2] T. Carlomagno,et al. An efficient strategy for the determination of the three-dimensional architecture of ribonucleoprotein complexes by the combination of a few easily accessible NMR and biochemical data: intermolecular recognition in a U4 spliceosomal complex. , 2009, Journal of molecular biology.
[3] P. Rosevear,et al. Protein global fold determination using site‐directed spin and isotope labeling , 2008, Protein science : a publication of the Protein Society.
[4] B. Simon,et al. Extending the Size of Protein–RNA Complexes Studied by Nuclear Magnetic Resonance Spectroscopy , 2005, Chembiochem : a European journal of chemical biology.
[5] J. Bushweller,et al. Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy. , 2006, Journal of the American Chemical Society.
[6] Jill Trewhella,et al. Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. , 2005, Journal of the American Chemical Society.
[7] Gottfried Otting,et al. Alignment of Biological Macromolecules in Novel Nonionic Liquid Crystalline Media for NMR Experiments , 2000 .
[8] G M Clore,et al. Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[9] C. Dominguez,et al. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. , 2003, Journal of the American Chemical Society.
[10] Oliver F. Lange,et al. Consistent blind protein structure generation from NMR chemical shift data , 2008, Proceedings of the National Academy of Sciences.
[11] Shigeyuki Yokoyama,et al. Solution structures of the first and second RNA‐binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF65) , 1999, The EMBO journal.
[12] A. Pardi,et al. Filamentous bacteriophage for aligning RNA, DNA, and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions. , 2000, Methods in enzymology.
[13] A. Pardi,et al. Refinement of local and long-range structural order in theophylline-binding RNA using (13)C-(1)H residual dipolar couplings and restrained molecular dynamics. , 2001, Journal of the American Chemical Society.
[14] Charles D Schwieters,et al. Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics. , 2003, Journal of the American Chemical Society.
[15] N. Tjandra,et al. Determination of the solution-bound conformation of an amino acid binding protein by NMR paramagnetic relaxation enhancement: use of a single flexible paramagnetic probe with improved estimation of its sampling space. , 2009, Journal of the American Chemical Society.
[16] Michael R Green,et al. Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65. , 2006, Molecular cell.
[17] Alexander N. Volkov,et al. Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR , 2006, Proceedings of the National Academy of Sciences.
[18] J. Prestegard,et al. Residual dipolar couplings in structure determination of biomolecules. , 2004, Chemical reviews.
[19] G. Marius Clore,et al. Visualization of transient encounter complexes in protein–protein association , 2006, Nature.
[20] Michele Vendruscolo,et al. Protein structure determination from NMR chemical shifts , 2007, Proceedings of the National Academy of Sciences.
[21] Marc Schoenauer,et al. A simple genetic algorithm for the optimization of multidomain protein homology models driven by NMR residual dipolar coupling and small angle X-ray scattering data , 2007, European Biophysics Journal.
[22] I. Bertini,et al. Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples. , 2009, Journal of the American Chemical Society.
[23] Michael Nilges,et al. Ambiguous NOEs and automated NOE assignment , 1998 .
[24] Ad Bax,et al. Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase , 1998 .
[25] A. Bax,et al. Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.
[26] D. Shortle,et al. Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. , 1997, Journal of molecular biology.
[27] J. Thornton,et al. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR , 1996, Journal of biomolecular NMR.
[28] M. Blackledge. Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings , 2005 .
[29] G. Wagner,et al. Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data. , 2000, Biochemistry.
[30] G. Clore,et al. Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. , 2009, Chemical reviews.
[31] Michael Nilges,et al. ARIA: automated NOE assignment and NMR structure calculation , 2003, Bioinform..
[32] G. Wagner,et al. Ribosome Loading onto the mRNA Cap Is Driven by Conformational Coupling between eIF4G and eIF4E , 2003, Cell.
[33] Gottfried Otting,et al. Prospects for lanthanides in structural biology by NMR , 2008, Journal of biomolecular NMR.
[34] Alexandre M J J Bonvin,et al. Various strategies of using residual dipolar couplings in NMR‐driven protein docking: Application to Lys48‐linked di‐ubiquitin and validation against 15N‐relaxation data , 2005, Proteins.
[35] Ivano Bertini,et al. Magnetic susceptibility in paramagnetic NMR , 2002 .
[36] J H Prestegard,et al. Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex. , 1999, Journal of molecular biology.