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Default High-resolution methyl edited GFT NMR experiments for protein resonance assignments a

High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.

Related Articles High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.

J Biomol NMR. 2010 Sep 14;

Authors: Jaipuria G, Thakur A, D'Silva P, Atreya HS

Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile, Leu, Met, Thr and Val) there is a significant overlap of (13)C and (1)H chemical shifts. Such overlap can be resolved using the recently proposed (3,2)D HCCH-COSY, a G-matrix Fourier transform (GFT) NMR based experiment, which facilitates editing of methyl groups into distinct spectral regions by combining their (13)C chemical shifts with that of the neighboring, directly attached, (13)C nucleus. Using this principle, we present three GFT experiments: (a) (4,3)D NOESY-HCCH, (b) (4,3)D (1)H-TOCSY-HCCH and (c) (4,3)D (13)C-TOCSY-HCCH. These experiments provide unique 4D spectral information rapidly with high sensitivity and resolution for side-chain resonance assignments and NOE analysis of methyl groups. This is exemplified by (4,3)D NOESY-HCCH data acquired for 17.9Â*kDa non-deuterated cytosolic human J-protein co-chaperone, which provided crucial long-range distance constraints for its 3D structure determination.

PMID: 20838855 [PubMed - as supplied by publisher]



Source: PubMed
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