Title: | Evidence of chemical exchange in recombinant Major Urinary Protein and quenching thereof upon pheromone binding |
Author(s): | Perazzolo C; Verde M; Homans SW; Bodenhausen G; |
Address: | "Institut des Sciences et Ingenierie Chimiques, Ecole Polytechnique Federale de Lausanne, 1015, Lausanne, Switzerland. Chiara.Perazzolo@epfl.ch" |
DOI: | 10.1007/s10858-006-9110-1 |
ISSN/ISBN: | 0925-2738 (Print) 0925-2738 (Linking) |
Abstract: | "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 beta-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" |
Keywords: | "Animals Computer Simulation Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular/methods Protein Binding Protein Structure, Secondary Proteins/*chemistry/genetics Pyrazines/chemistry Recombinant Proteins/*chemistry;" |
Notes: | "MedlinePerazzolo, Chiara Verde, Mariachiara Homans, Steve W Bodenhausen, Geoffrey eng Research Support, Non-U.S. Gov't Netherlands 2007/03/08 J Biomol NMR. 2007 May; 38(1):3-9. doi: 10.1007/s10858-006-9110-1. Epub 2007 Mar 7" |