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Effects of Protein-pheromone Complexation on Correlated Chemical Shift Modulations

Perazzolo, Chiara ; Wist, Julien ; Loth, Karine ; Poggi, Luisa ; Homans, Steve ; Bodenhausen, Geoffrey

In: Journal of Biomolecular NMR, 2005, vol. 33, no. 4, p. 233-242

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    Titel
    • Effects of Protein-pheromone Complexation on Correlated Chemical Shift Modulations
    Autor
    • Perazzolo, Chiara. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, BCH, Switzerland
    • Wist, Julien. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, BCH, Switzerland
    • Loth, Karine. Département de chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris cedex 05, France
    • Poggi, Luisa. Département de chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris cedex 05, France
    • Homans, Steve. School of Biochemistry and Microbiology, University of Leeds, Woodhouse Lane, LS2 9JT, Leeds, England
    • Bodenhausen, Geoffrey. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, 1015, Lausanne, BCH, Switzerland
    Dokumententyp
    • Postprint
    Sprache
    • Englisch
    Veröffentlicht in
    • Journal of Biomolecular NMR, 2005, vol. 33, no. 4, p. 233-242. Kluwer Academic Publishers
    Andere elektronische Ausgabe
    OAI-PMH-ID
    • oai:doc.rero.ch:319672
    Summary
    Major urinary protein (MUP) is a pheromone-carrying protein of the lipocalin family. Previous studies by isothermal titration calorimetry (ITC) show that the affinity of MUP for the pheromone 2-methoxy-3-isobutylpyrazine (IBMP) is mainly driven by enthalpy, with a small unfavourable entropic contribution. Entropic terms can be attributed in part to changes in internal motions of the protein upon binding. Slow internal motions can lead to correlated or anti-correlated modulations of the isotropic chemical shifts of carbonyl C′ and amide N nuclei. Correlated chemical shift modulations (CSM/CSM) in MUP have been determined by measuring differences of the transverse relaxation rates of zero- and double-quantum coherences ZQC{C′N} and DQC{C′N}, and by accounting for the effects of correlated fluctuations of dipole-dipole couplings (DD/DD) and chemical shift anisotropies (CSA/CSA). The latter can be predicted from tensor parameters of C′ and N nuclei that have been determined in earlier work. The effects of complexation on slow time-scale protein dynamics can be determined by comparing the temperature dependence of the relaxation rates of APO-MUP (i.e., without ligand) and HOLO-MUP (i.e., with IBMP as a ligand)