Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
about
NMR data collection and analysis protocol for high-throughput protein structure determination.Improving NMR protein structure quality by Rosetta refinement: A molecular replacement studyStructural characterization of the protein cce_0567 from Cyanothece 51142, a metalloprotein associated with nitrogen fixation in the DUF683 familyNMR structure of protein YvyC fromBacillus subtilisreveals unexpected structural similarity between two PFAM familiesStructural characterization of Burkholderia pseudomallei adenylate kinase (Adk): Profound asymmetry in the crystal structure of the ‘open’ stateSolution structure of Rv2377c-founding member of the MbtH-like protein familyInaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543cCrystal structure of cce_0566 fromCyanothece 51142, a protein associated with nitrogen fixation in the DUF269 familySolution structure of a putative FKBP-type peptidyl-propyl cis–trans isomerase from Giardia lambliaNMRFAM-SDF: a protein structure determination frameworkThe NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein foldA solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chlorideUnique opportunities for NMR methods in structural genomics.Advances in Nuclear Magnetic Resonance for Drug Discovery.Advances in protein NMR provided by the NIGMS Protein Structure Initiative: impact on drug discovery.(¹⁵N ± ¹³C') edited (4, 3)D-H(CC)CONH TOCSY and (4, 3)D-NOESY HNCO experiments for unambiguous side chain and NOE assignments of proteins with high shift degeneracy.A time-saving strategy for MAS NMR spectroscopy by combining nonuniform sampling and paramagnetic relaxation assisted condensed data collectionADAPT-NMR 3.0: utilization of BEST-type triple-resonance NMR experiments to accelerate the process of data collection and assignment.High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection.Clean absorption-mode NMR data acquisition.Clean absorption mode NMR data acquisition based on time-proportional phase incrementationAutomated resonance assignment of proteins: 6D APSY-NMR.Maximum Entropy Spectral Reconstruction of Non-Uniformly Sampled Data.Automated projection spectroscopy (APSY).Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies.Radial sampling for fast NMR: Concepts and practices over three decades.GFT projection NMR spectroscopy for proteins in the solid state.Development and application of aromatic [(13)C, (1)H] SOFAST-HMQC NMR experiment for nucleic acids.Signal enhancement for the sensitivity-limited solid state NMR experiments using a continuous, non-uniform acquisition schemeChemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis.G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignmentConvex accelerated maximum entropy reconstructionBackbone and side chain (1)H, (13)C, and (15)N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei.1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold.Fast acquisition of multidimensional NMR spectra of solids and mesophases using alternative sampling methods.Subrandom methods for multidimensional nonuniform sampling.Deterministic schedules for robust and reproducible non-uniform sampling in multidimensional NMR.Spectroscopy by integration of frequency and time domain information for fast acquisition of high-resolution dark spectra.High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases.Reduced dimensionality (4,3)D-hnCOCANH experiment: an efficient backbone assignment tool for NMR studies of proteins.
P2860
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P2860
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@ast
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@en
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@nl
type
label
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@ast
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@en
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@nl
prefLabel
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@ast
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@en
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@nl
P2093
P2860
P356
P1476
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
@en
P2093
Deok C Yeh
Dinesh K Sukumaran
Hunter N B Moseley
Thomas Szyperski
P2860
P304
P356
10.1073/PNAS.122224599
P407
P577
2002-06-01T00:00:00Z