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Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat nonspecific lipid transfer protein

¹ Centre de Biophysique Moléculaire, CNRS, 45071 Orléans cedex 02, France
² Laboratoire Commun de RMN, Service de Chimie Moléculaire, CEA/Saclay, 91191 Gif sur Yvette, France

Reprint requests to: Dr. Hervé Desvaux, Service de Chimie Moléculaire, CEA/Saclay, F-91191 Gif sur Yvette, France; e-mail: hdesvaux{at}Cea.fr; fax: 33-1-69-08-98-06.

Nonspecific lipid transfer protein from wheat is studied by liquid-state NMR in the presence of xenon. The gas–protein interaction is indicated by the dependence of the protein proton chemical shifts on the xenon pressure and formally confirmed by the first observation of magnetization transfer from laser-polarized xenon to the protein protons. Twenty-six heteronuclear nOes have allowed the characterization of four interaction sites inside the wheat ns-LTP cavity. Their locations are in agreement with the variations of the chemical shifts under xenon pressure and with solvation simulations. The richness of the information obtained by the noble gas with a nuclear polarization multiplied by 12,000 makes this approach based on dipolar cross-relaxation with laser-polarized xenon promising for probing protein hydrophobic pockets at ambient pressure.

Keywords: Laser-polarized xenon; SPINOE; wheat nonspecific lipid transfer protein; protein hydrophobic cavity

Abbreviations: FID, Free Induction Decay • Ns-LTP, nonspecific lipid transfer protein • nOe, nuclear Overhauser effect • NOESY, nuclear Overhauser effect spectroscopy • TOCSY, total correlation spectroscopy • SPINOE, spin polarization-induced nuclear Overhauser effect

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