Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples - Wikidata - wikimedia - TriplyDB

Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples

Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples

http://www.wikidata.org/entity/Q24633467

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Recommendations of the wwPDB NMR Validation Task Force Computational modeling of membrane proteins Sparse labeling of proteins: structural characterization from long range constraints Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods PDBStat: a universal restraint converter and restraint analysis software package for protein NMR Structure of Est3 reveals a bimodal surface with differential roles in telomere replication Structural Characterization of Interactions between the Double-Stranded RNA-Binding Zinc Finger Protein JAZ and Nucleic Acids A Mechanism for the Auto-inhibition of Hyperpolarization-activated Cyclic Nucleotide-gated (HCN) Channel Opening and Its Relief by cAMP Integrating solid-state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT Integrative NMR for biomolecular research Protein structure determination by combining sparse NMR data with evolutionary couplings Protein structure prediction from sequence variation Critical assessment of methods of protein structure prediction (CASP)--round x De novo protein structure determination from near-atomic-resolution cryo-EM maps Assessment of CASP10 contact-assisted predictions.Quality assessment of protein NMR structures.BCL::Fold--protein topology determination from limited NMR restraints.Protein NMR structures refined with Rosetta have higher accuracy relative to corresponding X-ray crystal structures A practical implicit solvent potential for NMR structure calculation.Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.A community resource of experimental data for NMR / X-ray crystal structure pairs.Large-scale determination of previously unsolved protein structures using evolutionary information ProCS15: a DFT-based chemical shift predictor for backbone and Cβ atoms in proteins.Contact-assisted protein structure modeling by global optimization in CASP11.Combining Evolutionary Information and an Iterative Sampling Strategy for Accurate Protein Structure Prediction.Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.Structure prediction using sparse simulated NOE restraints with Rosetta in CASP11.Critical assessment of methods of protein structure prediction: Progress and new directions in round XI.A protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Systematic evaluation of CS-Rosetta for membrane protein structure prediction with sparse NOE restraints.Protein structure refinement using a quantum mechanics-based chemical shielding predictor F 1 F 2-selective NMR spectroscopy.Applications of contact predictions to structural biology Improving 3D structure prediction from chemical shift data.The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family.Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information.Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies.High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids Structural insights into activation of the retinal L-type Ca²⁺ channel (Cav1.4) by Ca²⁺-binding protein 4 (CaBP4)

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P2860

Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples

http://www.wikidata.org/entity/Q24633467

description

2012 nî lūn-bûn

@nan

2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Determination of solution stru ...... R data from deuterated samples

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Determination of solution stru ...... R data from deuterated samples

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Determination of solution stru ...... R data from deuterated samples

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type

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Determination of solution stru ...... R data from deuterated samples

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Determination of solution stru ...... R data from deuterated samples

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Determination of solution stru ...... R data from deuterated samples

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prefLabel

Determination of solution stru ...... R data from deuterated samples

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Determination of solution stru ...... R data from deuterated samples

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Determination of solution stru ...... R data from deuterated samples

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PNAS.1203013109

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Proceedings of the National Academy of Sciences of the United States of America

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Determination of solution stru ...... R data from deuterated samples

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Asli Ertekin

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Hsiau-Wei Lee

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James M Aramini

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Nikolaos G Sgourakis

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Oliver F Lange

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Paolo Rossi

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Rong Xiao

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Thomas B Acton

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Yifan Song

http://www.w3.org/2001/XMLSchema#string

P2860

NMR structure determination for larger proteins using backbone-only data

High-resolution structure prediction and the crystallographic phase problem

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein

X-ray structure of sensory rhodopsin II at 2.1-A resolution

Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands

Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR

Dynamic thiolation–thioesterase structure of a non-ribosomal peptide synthetase

Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

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10873-8

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27

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109

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Gaetano T. Montelione

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2012-07-03T00:00:00Z

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228066961

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22733734

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