Solution NMR-derived global fold of a monomeric 82-kDa enzyme. - Wikidata - wikimedia - TriplyDB

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

http://www.wikidata.org/entity/Q33756699

about

Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts Atomic resolution structures ofEscherichia coliandBacillus anthracismalate synthase A: Comparison with isoform G and implications for structure-based drug discovery Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.Intermolecular Interactions in a 44 kDa Interferon−Receptor Complex Detected by Asymmetric Reverse-Protonation and Two-Dimensional NOESY Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering Observation of Intermolecular Interactions in Large Protein Complexes by 2D-Double Difference Nuclear Overhauser Enhancement Spectroscopy: Application to the 44 kDa Interferon–Receptor Complex PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ Emerging methodologies to investigate lipid-protein interactions The product complex of M. tuberculosis malate synthase revisited Effects of NMR spectral resolution on protein structure calculation Prediction of Protein Structure Using Surface Accessibility Data Protein structure determination by combining sparse NMR data with evolutionary couplings Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB Structural proteomics by NMR spectroscopy.A community resource of experimental data for NMR / X-ray crystal structure pairs.Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.Critical assessment of methods of protein structure prediction: Progress and new directions in round XI.Impact of 15N R2/R1 relaxation restraints on molecular size, shape, and bond vector orientation for NMR protein structure determination with sparse distance restraints Overview on the use of NMR to examine protein structure.4D solid-state NMR for protein structure determination.Extracellular domain nicotinic acetylcholine receptors formed by alpha4 and beta2 subunits.Deuterated protein folds obtained directly from unassigned nuclear overhauser effect data.Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Recombinant production of isotope-labeled peptides and spontaneous cyclization of amino-terminal glutamine into pyroglutamic acid.Solid-state NMR of proteins sedimented by ultracentrifugation.Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy.Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.Homology modeling of larger proteins guided by chemical shifts.Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins.Automated assignment in selectively methyl-labeled proteins.Increased resolution of aromatic cross peaks using alternate 13C labeling and TROSY.Solution NMR of large molecules and assemblies SAIL--stereo-array isotope labeling.Observation of molecular inhibition and binding structures of amyloid peptides.Identifying critical unrecognized sugar-protein interactions in GH10 xylanases from Geobacillus stearothermophilus using STD NMR.Structural Biology: A Century-long Journey into an Unseen World.Solution NMR Spectroscopy in Target-Based Drug Discovery.

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P2860

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

http://www.wikidata.org/entity/Q33756699

description

2005 nî lūn-bûn

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2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

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Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

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type

label

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

@ast

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

@en

prefLabel

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

@ast

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

@en

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PNAS.0407792102

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

P1476

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.

@en

P2093

Vitali Tugarinov

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Vladislav Yu Orekhov

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Wing-Yiu Choy

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P2860

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

Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications

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

Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

Solution structure and dynamics of the outer membrane enzyme PagP by NMR.

Structure of theEscherichia colimalate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution

Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1.Sox2.Hoxb1-DNA ternary transcription factor complex

Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution

Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance

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15637152

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