Journal of Biomolecular NMR

, Volume 48, Issue 4, pp 213–223

GFT projection NMR spectroscopy for proteins in the solid state

Authors

  • W. Trent Franks
    • Department of ChemistryUniversity of Illinois at Urbana-Champaign
  • Hanudatta S. Atreya
    • Department of ChemistryState University of New York at Buffalo
    • NMR Research CentreIndian Institute of Science
  • Thomas Szyperski
    • Department of ChemistryState University of New York at Buffalo
    • Department of ChemistryUniversity of Illinois at Urbana-Champaign
    • Department of BiochemistryUniversity of Illinois at Urbana-Champaign
    • Center for Biophysics and Computational BiologyUniversity of Illinois at Urbana-Champaign
Article

DOI: 10.1007/s10858-010-9451-7

Cite this article as:
Trent Franks, W., Atreya, H.S., Szyperski, T. et al. J Biomol NMR (2010) 48: 213. doi:10.1007/s10858-010-9451-7

Abstract

Recording of four-dimensional (4D) spectra for proteins in the solid state has opened new avenues to obtain virtually complete resonance assignments and three-dimensional (3D) structures of proteins. As in solution state NMR, the sampling of three indirect dimensions leads per se to long minimal measurement time. Furthermore, artifact suppression in solid state NMR relies primarily on radio-frequency pulse phase cycling. For an n-step phase cycle, the minimal measurement times of both 3D and 4D spectra are increased n times. To tackle the associated ‘sampling problem’ and to avoid sampling limited data acquisition, solid state G-Matrix Fourier Transform (SS GFT) projection NMR is introduced to rapidly acquire 3D and 4D spectral information. Specifically, (4,3)D (HA)CANCOCX and (3,2)D (HACA)NCOCX were implemented and recorded for the 6 kDa protein GB1 within about 10% of the time required for acquiring the conventional congeners with the same maximal evolution times and spectral widths in the indirect dimensions. Spectral analysis was complemented by comparative analysis of expected spectral congestion in conventional and GFT NMR experiments, demonstrating that high spectral resolution of the GFT NMR experiments enables one to efficiently obtain nearly complete resonance assignments even for large proteins.

Keywords

Magic-angle spinningChemical shift assignmentsGB1Correlation spectroscopy

Supplementary material

10858_2010_9451_MOESM1_ESM.docx (51 kb)
Supplementary material 1 (DOCX 51 kb)

Copyright information

© Springer Science+Business Media B.V. 2010