Fulltext

Evidence of chemical exchange in recombinant Major Urinary Protein and quenching thereof upon pheromone binding

Perazzolo, Chiara ; Verde, Mariachiara ; Homans, Steve ; Bodenhausen, Geoffrey

In: Journal of Biomolecular NMR, 2007, vol. 38, no. 1, p. 3-9

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    Titel
    • Evidence of chemical exchange in recombinant Major Urinary Protein and quenching thereof upon pheromone binding
    Autor
    • Perazzolo, Chiara. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, Switzerland
    • Verde, Mariachiara. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, Switzerland
    • Homans, Steve. Institute of Molecular and Cellular Biology, University of Leeds, Woodhouse Lane, LS2 9JT, Leeds, UK
    • Bodenhausen, Geoffrey. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, Switzerland
    Dokumententyp
    • Postprint
    Sprache
    • Englisch
    Veröffentlicht in
    • Journal of Biomolecular NMR, 2007, vol. 38, no. 1, p. 3-9. Kluwer Academic Publishers
    Andere elektronische Ausgabe
    OAI-PMH-ID
    • oai:doc.rero.ch:311916
    Summary
    The internal dynamics of recombinant Major Urinary Protein (rMUP) have been investigated by monitoring transverse nitrogen-15 relaxation using multiple-echo Carr-Purcell-Meiboom-Gill (CPMG) experiments. While the ligand-free protein (APO-rMUP) features extensive evidence of motions on the milliseconds time scale, the complex with 2-methoxy-3-isobutylpyrazine (HOLO-rMUP) appears to be much less mobile on this time scale. At 308K, exchange rates k ex=500-2000s−1 were typically observed in APO-rMUP for residues located adjacent to a β-turn comprising residues 83-87. These residues occlude an entry to the binding pocket and have been proposed to be a portal for ligand entry in other members of the lipocalin family, such as the retinol binding protein and the human fatty-acid binding protein. Exchange rates and populations are largely uncorrelated, suggesting local ‘breathing' motions rather than a concerted global conformational change