Speeding up sequence specific assignment of IDPs
 

Speeding up sequence specific assignment of IDPs


Abstract The characterization of intrinsically disordered proteins (IDPs) by NMR spectroscopy is made difficult by the extensive spectral overlaps. To overcome the intrinsic low-resolution of the spectra the introduction of high-dimensionality experiments is essential. We present here a set of high-resolution experiments based on direct 13C-detection which proved useful in the assignment of α-synuclein, a paradigmatic IDP. In particular, we describe the implementation of 4D HCBCACON, HCCCON, HCBCANCO, 4/5D HNCACON and HNCANCO and 3/4D HCANCACO experiments, specifically tailored for spin system identification and backbone resonances sequential assignment. The use of non-uniform-sampling in the indirect dimension and of the H-flip approach to achieve longitudinal relaxation enhancement rendered the experiments very practical.

• Content Type Journal Article
• Category Article
• Pages 1-9
• DOI 10.1007/s10858-012-9639-0
• Authors
  • Wolfgang Bermel, Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten, Germany
  • Ivano Bertini, CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
  • Isabella C. Felli, CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
  • Leonardo Gonnelli, CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
  • Wiktor KoźmiÅ?ski, Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw, Poland
  • Alessandro Piai, CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
  • Roberta Pierattelli, CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
  • Jan Stanek, Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw, Poland

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738

Source: Journal of Biomolecular NMR