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 - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27664132

about

Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I Dimer Contrast-Matched Small-Angle X-ray Scattering from a Heavy-Atom-Labeled Protein in Structure Determination: Application to a Lead-Substituted Calmodulin–Peptide Complex Solution Structure of CCP Modules 10–12 Illuminates Functional Architecture of the Complement Regulator, Factor H High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data Solution Structure of the IIAChitobiose-HPr Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase System Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings Using small angle solution scattering data in Xplor-NIH structure calculations NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.Coupling between overall rotational diffusion and domain motions in proteins and its effect on dielectric spectra.Solution NMR Experiment for Measurement of (15)N-(1)H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.The use of residual dipolar coupling in studying proteins by NMR.Sample preparation, data collection, and preliminary data analysis in biomolecular solution X-ray scattering Structural characterization of a flexible two-domain protein in solution using small angle X-ray scattering and NMR data.Measurement of the temperature of the resting rotor in analytical ultracentrifugation.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Local isotropic diffusion approximation for coupled internal and overall molecular motions in NMR spin relaxation.Structural NMR of protein oligomers using hybrid methods.Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings.Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR.Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy.The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.Conformational selection and substrate binding regulate the monomer/dimer equilibrium of the C-terminal domain of Escherichia coli enzyme I.Validation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS).Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method.Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures.Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm Structural basis for enzyme I inhibition by α-ketoglutarate.Thermodynamic dissection of large-scale domain motions coupled with ligand binding of enzyme I.Nuclear magnetic resonance analysis of protein-DNA interactions.Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering.Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.NMR methods for structural studies of large monomeric and multimeric proteins.Integrative computational modeling of protein interactions.

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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

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description

2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Journal of the American Chemical Society

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Solution Structure of the 128 ...... nd Wide-Angle X-ray Scattering

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Alexander Grishaev

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G Marius Clore

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Jeong-Yong Suh

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Yuki Takayama

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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

Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings

Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr

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

Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints

Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples

Crystal Structure of Enzyme I of the Phosphoenolpyruvate Sugar Phosphotransferase System in the Dephosphorylated State

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr

Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR

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13026-45

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10.1021/JA105485B

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37

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132

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Rodolfo Ghirlando

Charles D Schwieters

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2010-09-22T00:00:00Z

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45819534

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20731394

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Escherichia coli

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2955445

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