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Effects of protein-pheromone complexation on correlated chemical shift modulations

Lookup NU author(s): Professor Steve Homans


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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).

Publication metadata

Author(s): Perazzolo C, Wist J, Loth K, Poggi L, Homans SW, Bodenhausen G

Publication type: Article

Publication status: Published

Journal: Journal of Biomolecular NMR

Year: 2005

Volume: 33

Issue: 4

Pages: 233-242

ISSN (print): 0925-2738

ISSN (electronic): 1573-5001

Publisher: Springer Netherlands


DOI: 10.1007/s10858-005-3355-y


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