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Recommendations of the wwPDB NMR Validation Task ForceOpen-to-closed transition in apo maltose-binding protein observed by paramagnetic NMRRegulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3ɛ Cytoplasmic Tyrosine-Based MotifDetermination of Multicomponent Protein Structures in Solution Using Global Orientation and Shape RestraintsSolution structure of the cap-independent translational enhancer and ribosome-binding element in the 3' UTR of turnip crinkle virusSolution 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 ScatteringCombined 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 DimerHigh-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental datapH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRStructure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid BilayerThree-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain TissueStructure and Dynamics of Full-Length HIV-1 Capsid Protein in SolutionCold denaturation of a protein dimer monitored at atomic resolutionThe Xplor-NIH NMR molecular structure determination packageUsing small angle solution scattering data in Xplor-NIH structure calculationsCompletely automated, highly error-tolerant macromolecular structure determination from multidimensional nuclear overhauser enhancement spectra and chemical shift assignmentsAutomated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithmAssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.A practical implicit solvent potential for NMR structure calculation.A pseudopotential for improving the packing of ellipsoidal protein structures determined from NMR data.Protein structure refinement using 13C alpha chemical shift tensorsHigh quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.Impact of 15N R2/R1 relaxation restraints on molecular size, shape, and bond vector orientation for NMR protein structure determination with sparse distance restraintsParameterization of solvent-protein interaction and its use on NMR protein structure determinationSolution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridgingEnsemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule.NMR Exchange Format: a unified and open standard for representation of NMR restraint data.A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large-angle X-ray scattering data.Global molecular structure and interfaces: refining an RNA:RNA complex structure using solution X-ray scattering data.How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?Direct use of 15N relaxation rates as experimental restraints on molecular shape and orientation for docking of protein-protein complexes.Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data.Theoretical and computational advances in biomolecular NMR spectroscopy.Conjoined use of EM and NMR in RNA structure refinement.Coupling between internal dynamics and rotational diffusion in the presence of exchange between discrete molecular conformations.Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy.A Practical Implicit Membrane Potential for NMR Structure Calculations of Membrane Proteins.Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation.Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures.
P50
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P50
description
researcher ORCID ID = 0000-0002-4216-4658
@en
wetenschapper
@nl
name
Charles D Schwieters
@ast
Charles D Schwieters
@en
Charles D Schwieters
@es
Charles D Schwieters
@nl
type
label
Charles D Schwieters
@ast
Charles D Schwieters
@en
Charles D Schwieters
@es
Charles D Schwieters
@nl
prefLabel
Charles D Schwieters
@ast
Charles D Schwieters
@en
Charles D Schwieters
@es
Charles D Schwieters
@nl
P31
P496
0000-0002-4216-4658