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Progress in Nuclear Magnetic Resonance Spectroscopy, ISSN 0079-6565, 2008, Volume 53, Issue 4, pp. 208 - 226
Journal Article
FEBS Letters, ISSN 0014-5793, 12/2014, Volume 588, Issue 24, pp. 4583 - 4589
Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein abundantly expressed in the brain. Mutations in the gene are causative for... 
Intra-molecular interaction | NMR | Intrinsically disordered protein | Segmental isotope-labeling | Expressed protein ligation | EPL | polar amino acid-rich domain | PRD | matrix-assisted laser desorption ionization time-of-flight mass analysis | WW domain | expressed protein ligation | C-segment | PQBP1 | IDP | PQBP1(1–219) with a C-terminal thioester group | C-terminal domain | high-performance liquid chromatography | sodium dodecyl sulfate–polyacrylamide gel electrophoresis | HPLC | residues 1–219 of PQBP1 | PQBP1(220–265) with a Gly220Cys mutation | intrinsically disordered protein | sodium 2-sulfanylethanesulfonate | N-fragment | WWD | N-segment | residues 220–265 of PQBP1 | polyglutamine tract-binding protein 1 | SDS–PAGE | nuclear magnetic resonance | MALDI-TOF MS | CTD | MESNA | C-fragment | POLYGLUTAMINE TRACT | TERMINAL DOMAIN | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | NATIVE CHEMICAL LIGATION | TRANSCRIPTION | N-15 | CELL BIOLOGY | BIOPHYSICS | ASSIGNMENT | U5-15KD | TRACT-BINDING PROTEIN-1 | RESIDUES | Isotope Labeling | Nuclear Proteins - metabolism | Magnetic Resonance Spectroscopy | Nuclear Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Intrinsically Disordered Proteins - metabolism | Proteins | Medical research | Surface active agents | Analysis | Medicine, Experimental | Nuclear magnetic resonance spectroscopy | Sulfates | Labeling | Mental illness | High performance liquid chromatography | Protein binding | Index Medicus
Journal Article
Journal of Biomolecular NMR, ISSN 0925-2738, 1/2013, Volume 55, Issue 1, pp. 119 - 138
Human hnRNP A1 is a multi-functional protein involved in many aspects of nucleic-acid processing such as alternative splicing, micro-RNA biogenesis,... 
Biochemistry, general | Domain orientation | Biophysics and Biological Physics | RRM | Intein | Physics | Spectroscopy/Spectrometry | NMR | Segmental isotope labeling | UP1 | RNA recognition modes | Inter-domain interaction | HnRNP A1 | Structural biology | 13 C-edited half-filter NOESY | Expressed protein ligation | C-edited half-filter NOESY | BACKBONE DYNAMICS | SPLICING REGULATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TORSION ANGLE DYNAMICS | PRE-RIBOSOMAL-RNA | MACROMOLECULAR STRUCTURE DETERMINATION | MESSENGER-RNA | SPECTROSCOPY | HETERONUCLEAR NMR-SPECTROSCOPY | C-13-edited half-filter NOESY | RIBONUCLEOPROTEIN A1 | Humans | Models, Molecular | RNA, Messenger - metabolism | Heterogeneous Nuclear Ribonucleoprotein A1 | Amino Acid Motifs | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Isotope Labeling | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | RNA, Messenger - chemistry | Molecular Docking Simulation | Protein Interaction Domains and Motifs | Binding Sites | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Proteins | RNA | Nuclear magnetic resonance spectroscopy | Biosynthesis | Chemical properties | Glycine | Protein binding | Index Medicus | Alternative splicing | Crystals | Unwinding | Data processing | mRNA | nucleic acids | Magnetic resonance spectroscopy | N.M.R | Telomeres | Reviews | RNA transport | Isotopes | Crystal structure | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2008, Volume 375, Issue 1, pp. 151 - 164
The study of multidomain or large proteins in solution by NMR spectroscopy has been made possible in recent years by the development of new spectroscopic... 
expressed protein ligation | NMR | structural biology | segmental labeling | METHANOBACTERIUM-THERMOAUTOTROPHICUM | BIOLOGICAL MACROMOLECULES | BIOCHEMISTRY & MOLECULAR BIOLOGY | NATIVE CHEMICAL LIGATION | TRANSCRIPTION | COMPLEXES | ASSIGNMENT | NOESY | RNA RECOGNITION | CELL-FREE SYNTHESIS | INTEIN | Fungal Proteins - chemistry | RNA-Binding Proteins - genetics | Temperature | Molecular Weight | Models, Chemical | Nuclear Proteins - isolation & purification | Humans | Heterogeneous-Nuclear Ribonucleoprotein L - chemistry | Molecular Sequence Data | RNA-Binding Proteins - isolation & purification | Recombinant Fusion Proteins - metabolism | Heterogeneous-Nuclear Ribonucleoprotein L - isolation & purification | Nuclear Magnetic Resonance, Biomolecular | Saccharomyces cerevisiae Proteins - isolation & purification | Cysteine - metabolism | Heterogeneous-Nuclear Ribonucleoprotein L - genetics | Nuclear Proteins - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Nitrogen Isotopes - metabolism | Protein Structure, Secondary | Electrophoresis, Polyacrylamide Gel | RNA-Binding Proteins - chemistry | Models, Molecular | Nuclear Proteins - metabolism | Carbon Isotopes - metabolism | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Static Electricity | Amino Acid Motifs | Isotope Labeling - methods | Heterogeneous-Nuclear Ribonucleoprotein L - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Conformation | RNA-Binding Proteins - metabolism | Amino Acid Substitution | Hydrogen-Ion Concentration | Saccharomyces cerevisiae Proteins - chemistry | Nuclear magnetic resonance spectroscopy | Polypeptides | Tracers (Biology) | Ribosomal proteins | Methods | Index Medicus
Journal Article
Journal Article
Journal Article
Methods in Enzymology, ISSN 0076-6879, 2015, Volume 565, pp. 389 - 422
The steady technical advances of nuclear magnetic resonance (NMR) over the past decades enabled a significant increase in the molecular size of protein... 
Protein ligation | Cell-free protein expression | NMR spectroscopy | Amino acid-specific isotope labeling | Segmental isotope labeling | Expressed protein ligation | Isotope Labeling | Amino Acids - metabolism | Proteins - metabolism | Magnetic Resonance Spectroscopy | Index Medicus
Journal Article