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Journal Articles Proteins: Structure, Function, and Genetics Year : 1998

Exploring hydrophobic sites in proteins with xenon or krypton

Abstract

X-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures. These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination.

Dates and versions

hal-04021077 , version 1 (09-03-2023)

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Thierry Prangé, Marc Schiltz, Lucile Pernot, Nathalie Colloc'H, Sonia Longhi, et al.. Exploring hydrophobic sites in proteins with xenon or krypton. Proteins: Structure, Function, and Genetics, 1998, 30 (1), pp.61-73. ⟨10.1002/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.0.CO;2-N⟩. ⟨hal-04021077⟩
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