Referenced in: none

Automatically associated channels: Kv1.4

Title: An approach to NMR assignment of intrinsically disordered proteins.

Authors: Nishit Goradia, Christoph Wiedemann, Christian Herbst, Matthias Görlach, Stefan H Heinemann, Oliver Ohlenschläger, Ramadurai Ramachandran

Journal, date & volume: Chemphyschem, 2015 Mar 16 , 16, 739-46

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/25639453

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.