TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
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Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differencesThe Rac1 polybasic region is required for interaction with its effector PRK1Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micellesThe role of the Src homology 3-Src homology 2 interface in the regulation of Src kinasesSolution structure and stability of the full-length excisionase from bacteriophage HK022The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteinsX-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoateThe Apo-structure of the Low Molecular Weight Protein-tyrosine Phosphatase A (MptpA) from Mycobacterium tuberculosis Allows for Better Target-specific Drug DevelopmentFacile backbone structure determination of human membrane proteins by NMR spectroscopyRole of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJSolution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coliNMR analysis of a 900K GroEL GroES complexCytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMREffects of NMR spectral resolution on protein structure calculationBtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanismStructure-function analysis of a broad specificity Populus trichocarpa endo-β-glucanase reveals an evolutionary link between bacterial licheninases and plant XTH gene productsThe solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrinNMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.The occludin and ZO-1 complex, defined by small angle X-ray scattering and NMR, has implications for modulating tight junction permeability.Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles.NMR structures of polytopic integral membrane proteins.Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.NMR solution structure determination of membrane proteins reconstituted in detergent micelles.Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBIntroduction to NMR of proteins.NMR Backbone Assignment of Large Proteins by Using (13) Cα -Only Triple-Resonance Experiments.Confinement Alters the Structure and Function of Calmodulin.Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.Overview on the use of NMR to examine protein structure.Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMRNMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.Ligand binding study of human PEBP1/RKIP: interaction with nucleotides and Raf-1 peptides evidenced by NMR and mass spectrometry.Backbone resonance assignments for the cytoplasmic region of the Mg(2+) transporter MgtE in the Mg (2+)-unbound state.Structural insights into the interaction between a potent anti-inflammatory protein, viral CC chemokine inhibitor (vCCI), and the human CC chemokine, Eotaxin-1Quaternary structure of hemoglobin in solutionCluster and fold stability of E. coli ISC-type ferredoxin.
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P2860
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
description
im Februar 1999 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в лютому 1999
@uk
name
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@en
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@nl
type
label
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@en
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@nl
prefLabel
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@en
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@nl
P2093
P356
P1476
TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins
@en
P2093
Konstantin Pervushin
Michael Salzmann
P304
P356
10.1021/JA9834226
P407
P577
1999-02-01T00:00:00Z