par Locci, Emanuela 
;Dehouck, Yves ;Casu, Mariano;Saba, Giuseppe;Lai, Adolfo;Luhmer, Michel ;Reisse, Jacques ;Bartik, Kristin
Référence Journal of magnetic resonance, 150, 2, page (167-174)
Publication Publié, 2001-06
;Dehouck, Yves ;Casu, Mariano;Saba, Giuseppe;Lai, Adolfo;Luhmer, Michel ;Reisse, Jacques ;Bartik, Kristin Référence Journal of magnetic resonance, 150, 2, page (167-174)
Publication Publié, 2001-06
Article révisé par les pairs
| Résumé : | The interaction of xenon with different proteins in aqueous solution is investigated by (129)Xe NMR spectroscopy. Chemical shifts are measured in horse metmyoglobin, hen egg white lysozyme, and horse cytochrome c solutions as a function of xenon concentration. In these systems, xenon is in fast exchange between all possible environments. The results suggest that nonspecific interactions exist between xenon and the protein exteriors and the data are analyzed in term of parameters which characterize the protein surfaces. The experimental data for horse metmyoglobin are interpreted using a model in which xenon forms a 1:1 complex with the protein and the chemical shift of the complexed xenon is reported (Locci et al., Keystone Symposia "Frontiers of NMR in Molecular Biology VI", Jan. 9--15, 1999, Breckenridge, CO, Abstract E216, p. 53; Locci et al., XeMAT 2000 "Optical Polarization and Xenon NMR of Materials", June 28--30, 2000, Sestri Levante, Italy, p. 46). |
