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Probing Proteins in Solution by 129Xe NMR Spectroscopy

✍ Scribed by Emanuela Locci; Yves Dehouck; Mariano Casu; Giuseppe Saba; Adolfo Lai; Michel Luhmer; Jacques Reisse; Kristin Bartik

Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
136 KB
Volume
150
Category
Article
ISSN
1090-7807

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✦ Synopsis

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

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