Published March 2018 | Version v1
Journal article

13C APSY-NMR for sequential assignment of intrinsically disordered proteins

  • 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

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Copyright
Copyright (c) 2018 Springer Science+Business Media B.V., part of Springer Nature