1992Journal de Chimie PhysiqueRequires access

Application of homonuclear three-dimensional NMR spectroscopy to the study of a protein in solution

Serge Bouaziz, Carine van Heijenoort, Éric Guittet, J. Y. Lallemand

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Abstract

In the case of biological macromolecules of molecular weight superior to 10000 Da, two difficulties trouble in the bi-dimensional NMR spectrum interpretation (2D NMR). On the one hand, the larger number of protons leads to resonance overlap, on the other hand, agregation phenomena cause line broadening. A solution is to spread the information to a third dimension by performing homonuclear three-dimensional NMR (3D NMR) experiments. That allows improvement of the spectral resolution and increases the size of molecules amenable to structure determination by NMR spectroscopy.

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In the case of biological macromolecules of molecular weight superior to 10000 Da, two difficulties trouble in the bi-dimensional NMR spectrum interpretation (2D NMR). On the one hand, the larger number of protons leads to resonance overlap, on the other hand, agregation phenomena cause line broadening. A solution is to spread the information to a third dimension by performing homonuclear three-dimensional NMR (3D NMR) experiments. That allows improvement of the spectral resolution and increases the size of molecules amenable to structure determination by NMR spectroscopy.

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Available abstract

In the case of biological macromolecules of molecular weight superior to 10000 Da, two difficulties trouble in the bi-dimensional NMR spectrum interpretation (2D NMR). On the one hand, the larger number of protons leads to resonance overlap, on the other hand, agregation phenomena cause line broadening. A solution is to spread the information to a third dimension by performing homonuclear three-dimensional NMR (3D NMR) experiments. That allows improvement of the spectral resolution and increases the size of molecules amenable to structure determination by NMR spectroscopy.

Key concepts: Homonuclear molecule, Nuclear magnetic resonance spectroscopy, Spectroscopy, Macromolecule, Transverse relaxation-optimized spectroscopy, Chemistry, Nuclear magnetic resonance, Two-dimensional nuclear magnetic resonance spectroscopy

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