Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment. - Wikidata - awgldk - TriplyDB

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

http://www.wikidata.org/entity/Q34030851

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NMR data collection and analysis protocol for high-throughput protein structure determination.Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study Structural characterization of the protein cce_0567 from Cyanothece 51142, a metalloprotein associated with nitrogen fixation in the DUF683 family NMR structure of protein YvyC fromBacillus subtilisreveals unexpected structural similarity between two PFAM families Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): Profound asymmetry in the crystal structure of the ‘open’ state Solution structure of Rv2377c-founding member of the MbtH-like protein family Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c Crystal structure of cce_0566 fromCyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family Solution structure of a putative FKBP-type peptidyl-propyl cis–trans isomerase from Giardia lamblia NMRFAM-SDF: a protein structure determination framework The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold A solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chloride Unique 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 collection ADAPT-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 incrementation Automated 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 scheme Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis.G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment Convex accelerated maximum entropy reconstruction Backbone 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.

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P2860

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

http://www.wikidata.org/entity/Q34030851

description

2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

@ast

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

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Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

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type

label

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

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Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

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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.

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Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.

@en

P2093

Deok C Yeh

http://www.w3.org/2001/XMLSchema#string

Dinesh K Sukumaran

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Hunter N B Moseley

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Thomas Szyperski

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P2860

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

High-resolution solution NMR structure of the Z domain of staphylococcal protein A

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.

Automated analysis of NMR assignments and structures for proteins.

Protein NMR spectroscopy in structural genomics.

Reference deconvolution, phase correction, and line listing of NMR spectra by the 1D filter diagonalization method.

Three-dimensional (1)H-TOCSY-relayed ct-[(13)C, (1)H]-HMQC for aromatic spin system identification in uniformly (13)C-labeled proteins.

Fold assembly of small proteins using monte carlo simulations driven by restraints derived from multiple sequence alignments.

Automated analysis of protein NMR assignments using methods from artificial intelligence.

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scholarly article

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10.1073/PNAS.122224599

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12

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99

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Gaetano T. Montelione

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2002-06-01T00:00:00Z

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11313138

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12060747

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123011

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