Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
about
Chemical cross-linking and native mass spectrometry: A fruitful combination for structural biologyIntermolecular Interactions in a 44 kDa Interferon−Receptor Complex Detected by Asymmetric Reverse-Protonation and Two-Dimensional NOESYFacilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acidsPreparation, functional characterization, and NMR studies of human KCNE1, a voltage-gated potassium channel accessory subunit associated with deafness and long QT syndromeStructural characterization of the conformational change in calbindin-D28k upon calcium binding using differential surface modification analyzed by mass spectrometryNMR study of a membrane protein in detergent-free aqueous solution.Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy.Structural biology by NMR: structure, dynamics, and interactions.Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.The quiet renaissance of protein nuclear magnetic resonance.Extracellular domain nicotinic acetylcholine receptors formed by alpha4 and beta2 subunits.The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data.Deuterated protein folds obtained directly from unassigned nuclear overhauser effect data.Collecting single molecules with conventional optical tweezers.NMR analysis of G-protein betagamma subunit complexes reveals a dynamic G(alpha)-Gbetagamma subunit interface and multiple protein recognition modes.The STINT-NMR method for studying in-cell protein-protein interactions.Direct NMR observation of a substrate protein bound to the chaperonin GroEL.NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluidsPreparation of the modular multi-domain protein RPA for study by NMR spectroscopy.Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product releaseSmall peptide inhibitors disrupt a high-affinity interaction between cytoplasmic dynein and a viral cargo protein.NMR insights into folding and self-association of Plasmodium falciparum P2.Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.Amino acid selective unlabeling for sequence specific resonance assignments in proteins.N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.Structural characterization of triple transmembrane domain containing fragments of a yeast G protein-coupled receptor in an organic : aqueous environment by solution-state NMR spectroscopyNonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme.Carbonyl carbon label selective (CCLS) 1H-15N HSQC experiment for improved detection of backbone 13C-15N cross peaks in larger proteinsA solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase.Structural Mechanisms of Nucleosome Recognition by Linker Histones.The Structural Role of Antibody N-Glycosylation in Receptor InteractionsSulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90.Segmental isotopic labeling of ubiquitin chains to unravel monomer-specific molecular behaviorExtending the size of protein-RNA complexes studied by nuclear magnetic resonance spectroscopy.Methyl groups as probes of structure and dynamics in NMR studies of high-molecular-weight proteins.Sensitivity enhancement in static solid-state NMR experiments via single- and multiple-quantum dipolar coherencesNMR study of the tetrameric KcsA potassium channel in detergent micelles.Solution NMR of large molecules and assembliesNon-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins
P2860
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P2860
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@ast
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@en
type
label
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@ast
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@en
prefLabel
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@ast
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@en
P1476
Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.
@en
P2093
Peter M Hwang
Vitali Tugarinov
P304
P356
10.1146/ANNUREV.BIOCHEM.73.011303.074004
P50
P577
2004-01-01T00:00:00Z