An approach to sequential NMR assignments of proteins: application to chemical shift restraint-based structure prediction.
 

An approach to sequential NMR assignments of proteins: application to chemical shift restraint-based structure prediction.

Related Articles An approach to sequential NMR assignments of proteins: application to chemical shift restraint-based structure prediction.

J Biomol NMR. 2014 Jun 19;

Authors: Wiedemann C, Bellstedt P, Herbst C, Görlach M, Ramachandran R

Abstract
A procedure for the simultaneous acquisition of {HNCOCANH & HCCCONH} chemical shift correlation spectra employing sequential [Formula: see text] data acquisition for moderately sized proteins is presented. The suitability of the approach for obtaining sequential resonance assignments, including complete [Formula: see text] and [Formula: see text] chemical shift information, is demonstrated experimentally for a [Formula: see text] and [Formula: see text] labelled sample of the C-terminal winged helix (WH) domain of the minichromosome maintenance (MCM) complex of Sulfolobus solfataricus. The chemical shift information obtained was used to calculate the global fold of this winged helix domain via CS-Rosetta. This demonstrates that our procedure provides a reliable and straight-forward protocol for a quick global fold determination of moderately-sized proteins.


PMID: 24943494 [PubMed - as supplied by publisher]



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