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Default Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.

Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.

Related Articles Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.

J Biomol NMR. 2014 Jan 4;

Authors: Kovacs H, Gossert A

Abstract
Three improved (13)C-spinlock experiments for side chain assignments of isotope labelled proteins in liquid state are presented. These are based on wide bandwidth spinlock techniques that have become possible with contemporary cryogenic probes. The first application, the H(C(ali)C(aro))H-TOCSY, is an HCCH-TOCSY in which all CHn moieties of a protein are detected in a single experiment, including the aromatic ones. This enables unambiguous assignment of aromatic and aliphatic amino acids in a single, highly sensitive experiment. In the second application, the (13)C-detected C(all)-TOCSY, magnetization transfer comprises all carbons-aliphatic, aromatic as well as the carbonyl carbons-making the complete carbon assignment possible using one spectrum only. Thirdly, the frequently used HC(CCO)NH experiment was redesigned by replacing the long C-carbonyl refocused INEPT transfer step by direct (13)C-(13)C-TOCSY magnetization transfer from side chain carbons to the backbone carbonyls. The resulting HC(CCO)NH experiment minimizes relaxation losses because it is shorter and represents a more sensitive alternative particularly for larger proteins. The performance of the experiments is demonstrated on isotope labeled proteins up to the size of 43*kDa.


PMID: 24390406 [PubMed - as supplied by publisher]



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