Recent progress in NMR spectroscopy: toward the study of intrinsically disordered proteins of increasing size and complexity.
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pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteinsTyrosine phosphorylation within the intrinsically disordered cytosolic domains of the B-cell receptor: an NMR-based structural analysisIncreasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift ReagentDisProt 7.0: a major update of the database of disordered proteins.Targeting intrinsically disordered proteins in rational drug discovery.Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.Structural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions.Structural characterization of intrinsically disordered proteins by NMR spectroscopy.Caught in action: selecting peptide aptamers against intrinsically disordered proteins in live cells.An approach to NMR assignment of intrinsically disordered proteins.Detection of disordered regions in globular proteins using ¹³C-detected NMR.Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy.Can proteins be intrinsically disordered inside a membrane?Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins.Investigating Protein-Ligand Interactions by Solution Nuclear Magnetic Resonance Spectroscopy.Synergistic Regulation of Coregulator/Nuclear Receptor Interaction by Ligand and DNA.Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase.In-cell ¹³C NMR spectroscopy for the study of intrinsically disordered proteins.NMR structure analysis of uniformly 13C-labeled carbohydrates.Electron self-exchange of cytochrome c measured via13C detected protonless NMRExclusively Heteronuclear13C-Detected Amino-Acid-Selective NMR Experiments for the Study of Intrinsically Disordered Proteins (IDPs)
P2860
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P2860
Recent progress in NMR spectroscopy: toward the study of intrinsically disordered proteins of increasing size and complexity.
description
article científic
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article scientifique
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articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Recent progress in NMR spectro ...... ncreasing size and complexity.
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type
label
Recent progress in NMR spectro ...... ncreasing size and complexity.
@en
prefLabel
Recent progress in NMR spectro ...... ncreasing size and complexity.
@en
P2860
P356
P1433
P1476
Recent progress in NMR spectro ...... ncreasing size and complexity.
@en
P2860
P304
P356
10.1002/IUB.1045
P577
2012-05-04T00:00:00Z