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

Lookup NU author(s): Professor Steve Homans


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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 308 K, exchange rates k ex = 500–2000 s−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.

Publication metadata

Author(s): Perazzolo C, Verde M, Homans SW, Bodenhausen G

Publication type: Article

Publication status: Published

Journal: Journal of Biomolecular NMR

Year: 2007

Volume: 38

Issue: 1

Pages: 3-9

ISSN (print): 0925-2738

ISSN (electronic): 1573-5001

Publisher: Springer Netherlands


DOI: 10.1007/s10858-006-9110-1


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