An efficient protocol for NMR-spectroscopy-based structure determination of protein complexes in solution.

[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.