Document Detail

GFT projection NMR spectroscopy for proteins in the solid state.
MedLine Citation:
PMID:  21052779     Owner:  NLM     Status:  MEDLINE    
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.
W Trent Franks; Hanudatta S Atreya; Thomas Szyperski; Chad M Rienstra
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2010-10-30
Journal Detail:
Title:  Journal of biomolecular NMR     Volume:  48     ISSN:  1573-5001     ISO Abbreviation:  J. Biomol. NMR     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-11-22     Completed Date:  2011-02-28     Revised Date:  2014-09-17    
Medline Journal Info:
Nlm Unique ID:  9110829     Medline TA:  J Biomol NMR     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  213-23     Citation Subset:  IM    
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MeSH Terms
Bacterial Proteins / chemistry*
Fourier Analysis*
Nuclear Magnetic Resonance, Biomolecular / methods*
Protein Conformation
Proteins / chemistry*
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/IgG Fc-binding protein, Streptococcus; 0/Proteins

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