title: An approach to NMR assignment of intrinsically disordered proteins.
abstract: An efficient approach to NMR assignments in intrinsically disordered proteins is presented, making use of the good dispersion of cross peaks observed in [(15) N,(13) C']- and [(13) C',(1) H(N) ]-correlation spectra. The method involves the simultaneous collection of {3D (H)NCO(CAN)H and 3D (HACA)CON(CA)HA} spectra for backbone assignments via sequential H(N) and H(α) correlations and {3D (H)NCO(CACS)HS and 3D (HS)CS(CA)CO(N)H} spectra for side-chain (1) H and (13) C assignments, employing sequential (1) H data acquisitions with direct detection of both the amide and aliphatic protons. The efficacy of the approach for obtaining resonance assignments with complete backbone and side-chain chemical shifts is demonstrated experimentally for the 61-residue [(13) C,(15) N]-labelled peptide of a voltage-gated potassium channel protein of the Kv1.4 channel subunit. The general applicability of the approach for the characterisation of moderately sized globular proteins is also demonstrated.
authors: Biomolecular NMR Spectroscopy, Leibniz Institute for Age Research, Beutenbergstr. 11, 07745 Jena (Germany).
authors: Nishit
authors: N
authors: Goradia
authors: Christoph
authors: C
authors: Wiedemann
authors: Christian
authors: C
authors: Herbst
authors: Matthias
authors: M
authors: Görlach
authors: Stefan H
authors: SH
authors: Heinemann
authors: Oliver
authors: O
authors: Ohlenschläger
authors: Ramadurai
authors: R
authors: Ramachandran
mesh_terms: D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods* / Q000592:standards; D012015:Reference Standards
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: haem regulatory motifs; intrinsically disordered proteins; ion channels; nmr spectroscopy; sequential data acquisition