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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
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