Abstract
Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein abundantly expressed in the brain. Mutations in the PQBP1 gene are causative for X-linked mental retardation disorders. Here, we investigated the structure of the C-terminal segment within the context of full-length PQBP1. We produced a segmentally isotope-labeled PQBP1 composed of a non-labeled segment (residues 1-219; N-segment) and a 13C/15N-labeled segment (residues 220-265; C-segment). Our results demonstrate that the segmental isotope-labeling combined with NMR spectroscopy is useful for detecting a very weak intra-molecular interaction in an intrinsically disordered protein.
Original language | English |
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Pages (from-to) | 4583-4589 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 588 |
Issue number | 24 |
DOIs | |
State | Published - 2014/12/20 |
Keywords
- Expressed protein ligation
- Intra-molecular interaction
- Intrinsically disordered protein
- NMR
- Segmental isotope-labeling
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology