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Efficient determination of angles subtended by Cα-Hα and N-HN vectors in proteins via dipole-dipole cross-correlation§

Pelupessy, Philippe ; Chiarparin, Elisabetta ; Ghose, Ranajeet ; Bodenhausen, Geoffrey

In: Journal of Biomolecular NMR, 1999, vol. 13, no. 4, p. 375-380

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    Title
    • Efficient determination of angles subtended by Cα-Hα and N-HN vectors in proteins via dipole-dipole cross-correlation§
    Author
    • Pelupessy, Philippe. Section de Chimie, Université de Lausanne, BCH, CH-1015, Lausanne, Switzerland
    • Chiarparin, Elisabetta. Section de Chimie, Université de Lausanne, BCH, CH-1015, Lausanne, Switzerland
    • Ghose, Ranajeet. Section de Chimie, Université de Lausanne, BCH, CH-1015, Lausanne, Switzerland
    • Bodenhausen, Geoffrey. Section de Chimie, Université de Lausanne, BCH, CH-1015, Lausanne, Switzerland
    Document Type
    • Postprint
    Language
    • English
    Published in
    • Journal of Biomolecular NMR, 1999, vol. 13, no. 4, p. 375-380. Kluwer Academic Publishers
    Other Version
    OAI-PMH Identifier
    • oai:doc.rero.ch:320937
    Summary
    The angle ΘCαHα,NHN subtended by the internuclear vectors 13Cα-Hα and 15N-HN in doubly-labeled proteins can be determined by observing the effect of cross-correlation between the dipolar interactions on zero- and double-quantum coherences involving 13Cα and 15N. Two complementary 2D experiments with the appearance of 15N-HN correlation spectra yield signal intensities that depend on the rate of interconversion through cross-correlated relaxation of in-phase and doubly antiphase zero- and double-quantum coherences. The ratio of the signal intensities in the two experiments bears a simple relationship to the cross-correlation rate, and hence to the angle ΘCαHα,NHN. Assuming planarity of the peptide bond, the dihedral angle Ψ (between Cα and C′) can be determined from the knowledge of ΘCαHα,NHN. The experiments are very time-effective and provide good sensitivity and excellent spectral resolution