Probability-based protein secondary structure identification using combined NMR chemical-shift data
about
HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexesNMR solution structure of poliovirus uridylyated peptide linked to the genome (VPgpU)A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNACharacterization of protein secondary structure from NMR chemical shiftsTALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shiftsGibbs sampling and helix-cap motifsPlasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuSThe basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNAProbabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy13C NMR reveals no evidence of n-π* interactions in proteinsLigand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosisThe common structural architecture of Shigella flexneri and Salmonella typhimurium type three secretion needlesEngineering amyloid-like assemblies from unstructured peptides via site-specific lipid conjugationConformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteriaStructure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1.Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathwaySolid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural HeterogeneityFractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity.The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein.Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin.SimShift: identifying structural similarities from NMR chemical shifts.Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillationNeighboring residue effects in terminally blocked dipeptides: implications for residual secondary structures in intrinsically unfolded/disordered proteins.Conformational transitions of the cross-linking domains of elastin during self-assemblyUse of 13Calpha chemical shifts in protein structure determinationFactors affecting the use of 13C(alpha) chemical shifts to determine, refine, and validate protein structuresCSI 2.0: a significantly improved version of the Chemical Shift Index.A structured loop modulates coupling between the substrate-binding and dimerization domains in the multidrug resistance transporter EmrE.Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Performance of density functional models to reproduce observed (13)C(alpha) chemical shifts of proteins in solutionIn situ structural studies of Anabaena sensory rhodopsin in the E. coli membrane.PPM_One: a static protein structure based chemical shift predictor.Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieusQuantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry.NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination.Rapid prediction of multi-dimensional NMR data sets.Application of data mining tools for classification of protein structural class from residue based averaged NMR chemical shifts13C, 2h NMR studies of structural and dynamical modifications of glucose-exposed porcine aortic elastin.Accessible surface area from NMR chemical shifts.
P2860
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P2860
Probability-based protein secondary structure identification using combined NMR chemical-shift data
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին 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
Probability-based protein seco ...... mbined NMR chemical-shift data
@ast
Probability-based protein seco ...... mbined NMR chemical-shift data
@en
Probability-based protein seco ...... mbined NMR chemical-shift data
@nl
type
label
Probability-based protein seco ...... mbined NMR chemical-shift data
@ast
Probability-based protein seco ...... mbined NMR chemical-shift data
@en
Probability-based protein seco ...... mbined NMR chemical-shift data
@nl
prefLabel
Probability-based protein seco ...... mbined NMR chemical-shift data
@ast
Probability-based protein seco ...... mbined NMR chemical-shift data
@en
Probability-based protein seco ...... mbined NMR chemical-shift data
@nl
P2860
P356
P1433
P1476
Probability-based protein seco ...... mbined NMR chemical-shift data
@en
P2093
Oleg Jardetzky
Yunjun Wang
P2860
P304
P356
10.1110/PS.3180102
P407
P577
2002-04-01T00:00:00Z