about
Structural genomics of membrane proteinsNMR data collection and analysis protocol for high-throughput protein structure determination.Protein production and purificationTraditional biomolecular structure determination by NMR spectroscopy allows for major errors.Solution NMR structure of the 30S ribosomal protein S28E fromPyrococcus horikoshiiFully automated high-quality NMR structure determination of small 2H-enriched proteinsApplying an empirical hydropathic forcefield in refinement may improve low-resolution protein X-ray crystal structuresEffects of NMR spectral resolution on protein structure calculationProtein Crystallography from the Perspective of Technology DevelopmentsThe NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein foldStructural proteomics by NMR spectroscopy.Hydrogen-deuterium exchange mass spectrometry for determining protein structural changes in drug discovery.NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination.NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.A novel strategy for NMR resonance assignment and protein structure determination.Ultra-small-sample molecular structure detection using microslot waveguide nuclear spin resonance.Connecting nanoscale images of proteins with their genetic sequences.Contact replacement for NMR resonance assignmentImproving small-angle X-ray scattering data for structural analyses of the RNA worldReduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.A cell-free protein synthesis system for high-throughput proteomicsStructural genomics in endocrinology.JPred4: a protein secondary structure prediction server.Changes in signal transducer and activator of transcription 3 (STAT3) dynamics induced by complexation with pharmacological inhibitors of Src homology 2 (SH2) domain dimerization.Utilizing NMR to study the structure of growth-inhibitory proteins.Determination of protein backbone structures from residual dipolar couplings.Backbone solution structures of proteins using residual dipolar couplings: application to a novel structural genomics target.Molecular recognition in the case of flexible targets.Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assemblyG-matrix Fourier transform NMR spectroscopy for complete protein resonance assignmentAutomated protein fold determination using a minimal NMR constraint strategy.SAIL--stereo-array isotope labeling.Characterizing rapid, activity-linked conformational transitions in proteins via sub-second hydrogen deuterium exchange mass spectrometry.Fast automated NMR spectroscopy of short-lived biological samples.Amino acid biosynthesis and metabolic flux profiling of Pichia pastoris.Accurate prediction of interfacial residues in two-domain proteins using evolutionary information: implications for three-dimensional modeling.High-throughput screening of structural proteomics targets using NMR.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Protein NMR spectroscopy in structural genomics.
@ast
Protein NMR spectroscopy in structural genomics.
@en
Protein NMR spectroscopy in structural genomics.
@nl
type
label
Protein NMR spectroscopy in structural genomics.
@ast
Protein NMR spectroscopy in structural genomics.
@en
Protein NMR spectroscopy in structural genomics.
@nl
prefLabel
Protein NMR spectroscopy in structural genomics.
@ast
Protein NMR spectroscopy in structural genomics.
@en
Protein NMR spectroscopy in structural genomics.
@nl
P2093
P356
P1476
Protein NMR spectroscopy in structural genomics.
@en
P2093
Gunsalus KC
Montelione GT
Szyperski T
P304
P356
10.1038/80768
P478
P577
2000-11-01T00:00:00Z