Related ArticlesStructures of protein-protein complexes are docked using only NMR restraints from residual dipolar coupling and chemical shift perturbations.
J Am Chem Soc. 2002 Mar 13;124(10):2104-5
Authors: McCoy MA, Wyss DF
NMR structures of protein-protein and protein-ligand complexes rely heavily on intermolecular NOEs. Recent work has shown that if no significant conformational changes occur upon complex formation residual dipolar coupling can replace most of the NOE restraints in protein-protein complexes, while restraints derived from chemical shift perturbations can largely replace intermolecular NOEs in protein-ligand structures. By combining restraints from chemical shift perturbations with orientation restraints derived from measurements of residual dipolar couplings, we show that the structure of the EIN-HPr complex can be calculated without NOE restraints. The final structure, built from the crystal structures of EIN and HPr in their uncomplexed form and docked only with NMR restraints, places HPr within 2.5 A of the position determined from the mean NMR structure of the complex.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
J Am Chem Soc. 2011 Apr 4;
Authors: Ryabov Y, Schwieters CD, Clore GM
(15)N R(2)/R(1) relaxation data contain information on molecular shape and size as well as on bond vector orientations relative to...
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Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Yaroslav Ryabov, Charles D. Schwieters and G. Marius Clore
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201020c/aop/images/medium/ja-2011-01020c_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201020c
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http://feeds.feedburner.com/~r/acs/jacsat/~4/3J1IyCLkQMQ
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[NMR paper] GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.
GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.
Related Articles GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.
Protein Sci. 1998 Feb;7(2):491-9
Authors: Bayley MJ, Jones G, Willett P, Williamson MP
We report the development and validation of the program GENFOLD, a genetic algorithm that calculates protein structures using restraints obtained from NMR, such as distances derived from nuclear Overhauser effects, and dihedral angles derived from coupling constants. The program...
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[NMR paper] Determining the structures of large proteins and protein complexes by NMR.
Determining the structures of large proteins and protein complexes by NMR.
Related Articles Determining the structures of large proteins and protein complexes by NMR.
Trends Biotechnol. 1998 Jan;16(1):22-34
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess...
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[NMR paper] NMR structures of proteins and protein complexes beyond 20,000 M(r).
NMR structures of proteins and protein complexes beyond 20,000 M(r).
Related Articles NMR structures of proteins and protein complexes beyond 20,000 M(r).
Nat Struct Biol. 1997 Oct;4 Suppl:849-53
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.
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[NMR paper] Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dime
Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Related Articles Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Prog Biophys Mol Biol. 1994;62(2):153-84
Authors: Clore GM, Gronenborn AM
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[NMR paper] Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dime
Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Related Articles Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Prog Biophys Mol Biol. 1994;62(2):153-84
Authors: Clore GM, Gronenborn AM
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[NMR paper] NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and co
NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Related Articles NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Q Rev Biophys. 1999 Feb;32(1):57-98
Authors: Härd T
Structures of protein-protein complexes are docked using only NMR restraints from res
Linear Mode
