Journal of Biomolecular NMR

, Volume 59, Issue 4, pp 211–217 | Cite as

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

  • Christoph Wiedemann
  • Peter Bellstedt
  • Christian Herbst
  • Matthias Görlach
  • Ramadurai Ramachandran
Communication

Abstract

A procedure for the simultaneous acquisition of {HNCOCANH & HCCCONH} chemical shift correlation spectra employing sequential \(^{1}\hbox {H}\) data acquisition for moderately sized proteins is presented. The suitability of the approach for obtaining sequential resonance assignments, including complete \(^{15}\hbox {N}{},\, ^{1}\hbox {H}{}^{N},\, ^{13}\hbox {CO}{},\, ^{13}\hbox {C}^{\alpha }{},\, ^{13}\hbox {C}^{\beta }\) and \(^{1}\hbox {H}^{\alpha }\) chemical shift information, is demonstrated experimentally for a \(^{13}\hbox {C}\) and \(^{15}\hbox {N}\) 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.

Keywords

Protein structure prediction Sequential data acquisition Protein resonance assignment CS-Rosetta Winged helix domain 

Supplementary material

10858_2014_9842_MOESM1_ESM.pdf (2.1 mb)
Supplementary material 1 (pdf 2163 KB)

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Copyright information

© Springer Science+Business Media Dordrecht 2014

Authors and Affiliations

  • Christoph Wiedemann
    • 1
  • Peter Bellstedt
    • 1
  • Christian Herbst
    • 2
  • Matthias Görlach
    • 1
  • Ramadurai Ramachandran
    • 1
  1. 1.Biomolecular NMR SpectroscopyLeibniz Institute for Age Research - Fritz Lipmann InstituteJenaGermany
  2. 2.Department of PhysicsUbon Ratchathani UniversityUbon RatchathaniThailand

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