Optimization of Three-Dimensional TROSY-Type HCCH NMR Correlation of Aromatic ¹H–¹³C Groups in Proteins

Authors: Meissner A.; Sørensen O.W.

Source: Journal of Magnetic Resonance, Volume 139, Number 2, August 1999 , pp. 447-450(4)

Publisher: Academic Press

Abstract:

Improved methods for three-dimensional TROSY-Type HCCH correlation involving protons of negligible CSA are presented. The TROSY approach differs from the conventional approach of heteronuclear decoupling in evolution and detection periods by not mixing fast and slowly relaxing coherences and usually suppressing the former. Pervushin et al. (J. Am. Chem. Soc. 120, 6394–6400 (1998)) have proposed a 3D TROSY-type HCCH experiment where the TROSY approach is applied only in one of the ¹³C dimensions. A new pulse sequence applying the TROSY approach in both indirect dimensions is advantageous when the TROSY effect of the carbons is large or when a relatively high resolution is required. For lower resolutions or moderate TROSY effects we show that it is possible to combine the best of both worlds, namely to suppress heteronuclear couplings without mixing fast and slowly relaxing coherences while at the same time superimpose the two components and thus have both contribute to the detected signal. That is possible using the novel technique of Spin-State-Selective Time-Proportional Phase Incrementation (S³ TPPI). The new 3D S³ TPPI TROSY HCCH method is demonstrated on a ¹³C,¹⁵N-labeled protein sample, RAP 18–112 (N-terminal domain of ₂-macroglobulin receptor associated protein), at 750 MHz and average sensitivity enhancements of 10% are obtained for the cross peaks in comparison to methods based on conventional decoupling on one of the carbons or on TROSY on both carbons. Copyright 1999 Academic Press.

Language: English

Document Type: Miscellaneous

Affiliations: Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, Valby, DK-2500, Denmark

Publication date: 1999-08-01

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