Probability-based protein secondary structure identification using combined NMR chemical-shift data - Wikidata - awgldk - TriplyDB

Probability-based protein secondary structure identification using combined NMR chemical-shift data

Probability-based protein secondary structure identification using combined NMR chemical-shift data

http://www.wikidata.org/entity/Q24645154

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HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes NMR 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 RNA Characterization of protein secondary structure from NMR chemical shifts TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts Gibbs sampling and helix-cap motifs Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS The basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy 13C NMR reveals no evidence of n-π* interactions in proteins Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis The common structural architecture of Shigella flexneri and Salmonella typhimurium type three secretion needles Engineering amyloid-like assemblies from unstructured peptides via site-specific lipid conjugation Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria Structure 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 pathway Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity Fractional 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 fibrillation Neighboring 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-assembly Use of 13Calpha chemical shifts in protein structure determination Factors affecting the use of 13C(alpha) chemical shifts to determine, refine, and validate protein structures CSI 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 solution In 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 milieus Quantitative 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 shifts 13C, 2h NMR studies of structural and dynamical modifications of glucose-exposed porcine aortic elastin.Accessible surface area from NMR chemical shifts.

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P2860

Probability-based protein secondary structure identification using combined NMR chemical-shift data

http://www.wikidata.org/entity/Q24645154

description

2002 nî lūn-bûn

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2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2002 թվականի ապրիլին 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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Probability-based protein seco ...... mbined NMR chemical-shift data

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Probability-based protein seco ...... mbined NMR chemical-shift data

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Probability-based protein seco ...... mbined NMR chemical-shift data

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Probability-based protein seco ...... mbined NMR chemical-shift data

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Protein Science

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Probability-based protein seco ...... mbined NMR chemical-shift data

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Oleg Jardetzky

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Yunjun Wang

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P2860

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

1H, 13C and 15N chemical shift referencing in biomolecular NMR

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

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

Knowledge-based protein secondary structure assignment

Describing protein structure: a general algorithm yielding complete helicoidal parameters and a unique overall axis.

Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView.

Evaluation and improvement of multiple sequence methods for protein secondary structure prediction.

Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure.

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10.1110/PS.3180102

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11910028

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protein structure

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2373532

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