Published March 2018
| Version v1
Journal article
13C APSY-NMR for sequential assignment of intrinsically disordered proteins
Creators
- 1. CERM, University of Florence (Italy)
- 2. Bruker BioSpin GmbH (Germany)
Description
The increasingly recognized biological relevance of intrinsically disordered proteins requires a continuous expansion of the tools for their characterization via NMR spectroscopy, the only technique so far able to provide atomic-resolution information on these highly mobile macromolecules. Here we present the implementation of projection spectroscopy in 13C-direct detected NMR experiments to achieve the sequence specific assignment of IDPs. The approach was used to obtain the complete backbone assignment at high temperature of α-synuclein, a paradigmatic intrinsically disordered protein.
Additional details
Identifiers
Publishing Information
- Journal Title
- Journal of Biomolecular NMR
- Journal Volume
- 70
- Journal Issue
- 3
- Journal Page Range
- p. 167-175
- ISSN
- 0925-2738
INIS
- Country of Publication
- Netherlands
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 49100243
- Subject category
- S37: INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY;
- Descriptors DEI
- ALLOCATIONS; CARBON 13; NUCLEAR MAGNETIC RESONANCE; TEMPERATURE RANGE 0400-1000 K
- Descriptors DEC
- CARBON ISOTOPES; EVEN-ODD NUCLEI; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; NUCLEI; RESONANCE; STABLE ISOTOPES; TEMPERATURE RANGE
Optional Information
- Copyright
- Copyright (c) 2018 Springer Science+Business Media B.V., part of Springer Nature