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
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Speeding up sequence specific assignment of IDPs
Linear Mode
