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.

13C APSY-NMR for sequential assignment of intrinsically disordered proteins / Murrali, Maria Grazia; Schiavina, Marco; Sainati, Valerio; Bermel, Wolfgang; Pierattelli, Roberta; Felli, Isabella C.. - In: JOURNAL OF BIOMOLECULAR NMR. - ISSN 0925-2738. - STAMPA. - 70:(2018), pp. 167-175. [10.1007/s10858-018-0167-4]

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

MURRALI, MARIA GRAZIA;SCHIAVINA, MARCO;Pierattelli, Roberta
;
Felli, Isabella C.
2018

Abstract

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.
70
167
175
Murrali, Maria Grazia; Schiavina, Marco; Sainati, Valerio; Bermel, Wolfgang; Pierattelli, Roberta; Felli, Isabella C.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/1119581
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