Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
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NMR structure determination for larger proteins using backbone-only dataDetermination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samplesDirect and Propagated Effects of Small Molecules on Protein-Protein Interaction NetworksSolution structure of a paradigm ArsR family zinc sensor in the DNA-bound stateIntermolecular Interactions in a 44 kDa Interferon−Receptor Complex Detected by Asymmetric Reverse-Protonation and Two-Dimensional NOESYFully automated high-quality NMR structure determination of small 2H-enriched proteinsRole of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJUse of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solutionStructure and mutagenesis of the Dbl homology domainStructural characterization of the interaction of human lactoferrin with calmodulinProtein structure determination by combining sparse NMR data with evolutionary couplingsTemperature dependence of cross-effect dynamic nuclear polarization in rotating solids: advantages of elevated temperatures.Optimal degree of protonation for ¹H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency.Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins.NMR solution structure determination of membrane proteins reconstituted in detergent micelles.Identification of the regions involved in DNA binding by the mouse PEBP2alpha protein.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBDe novo protein structure generation from incomplete chemical shift assignments.A community resource of experimental data for NMR / X-ray crystal structure pairs.Critical assessment of methods of protein structure prediction: Progress and new directions in round XI.Advances in protein NMR provided by the NIGMS Protein Structure Initiative: impact on drug discovery.Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.Impact of 15N R2/R1 relaxation restraints on molecular size, shape, and bond vector orientation for NMR protein structure determination with sparse distance restraintsDeuterated protein folds obtained directly from unassigned nuclear overhauser effect data.High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.NMR reveals pathway for ferric mineral precursors to the central cavity of ferritinHydrophobic side chain dynamics of a glutamate receptor ligand binding domainTechniques and applications of NMR to membrane proteins.Methyl labeling and TROSY NMR spectroscopy of proteins expressed in the eukaryote Pichia pastoris.Extending the size limit of protein nuclear magnetic resonance.Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins.Deuterium isotope shifts for backbone ¹H, ¹⁵N and ¹³C nuclei in intrinsically disordered protein α-synucleinProtein global fold determination using site-directed spin and isotope labeling.StAR-related lipid transfer domain protein 5 binds primary bile acids.Automated protein fold determination using a minimal NMR constraint strategy.Solution NMR of large molecules and assembliesIn vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy.Interaction of the IkappaBalpha C-terminal PEST sequence with NF-kappaB: insights into the inhibition of NF-kappaB DNA binding by IkappaBalpha.Deuterium spin probes of backbone order in proteins: 2H NMR relaxation study of deuterated carbon alpha sites.The dynamic duo: combining NMR and small angle scattering in structural biology.
P2860
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P2860
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
description
im Februar 1997 veröffentlicher wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в лютому 1997
@uk
name
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@en
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@nl
type
label
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@en
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@nl
prefLabel
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@en
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@nl
P356
P1433
P1476
Global Folds of Highly Deuterated, Methyl-Protonated Proteins by Multidimensional NMR†
@en
P2093
Kevin H. Gardner
Michael K. Rosen
P304
P356
10.1021/BI9624806
P407
P50
P577
1997-02-01T00:00:00Z