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TROSY experiment for refinement of backbone ψ and φ by simultaneous measurements of cross-correlated relaxation rates and 3,4 J HαHN coupling constants

Vögeli, Beat ; Pervushin, Konstantin

In: Journal of Biomolecular NMR, 2002, vol. 24, no. 4, p. 291-300

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    Titre
    • TROSY experiment for refinement of backbone ψ and φ by simultaneous measurements of cross-correlated relaxation rates and 3,4 J HαHN coupling constants
    Auteur
    • Vögeli, Beat. Laboratorium für Physikalische Chemie, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093, Zürich, Switzerland
    • Pervushin, Konstantin. Laboratorium für Physikalische Chemie, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093, Zürich, Switzerland
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • Journal of Biomolecular NMR, 2002, vol. 24, no. 4, p. 291-300. Kluwer Academic Publishers
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:311689
    Summary
    The TROSY principle has been introduced into a HNCA experiment, which is designed for measurements of the intraresidual and sequential Hα-Cα/HN-N dipole/dipole and Hα-Cα/N dipole/CSA cross-correlated relaxation rates. In addition, the new experiment provides values of the 3,4 J Hα HN coupling constants measured in an E.COSY manner. The conformational restraints for the ψ and φ angles are obtained through the use of the cross-correlated relaxation rates together with the Karplus-type dependencies of the coupling constants. Improved signal-to-noise is achieved through preservation of all coherence transfer pathways and application of the TROSY principle. The application of the [15N,13C]-DQ/ZQ-[15N,1H]-TROSY-E.COSY experiment to the 16kDa apo-form of the E.coli Heme Chaperon protein CcmE is described. Overall good agreement is achieved between ψ and φ angles measured with the new experiment and the average values determined from an ensemble of 20 NMR conformers