Browse by author
Lookup NU author(s): Professor Steve Homans
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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).
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
URL: http://dx.doi.org/10.1007/s10858-005-3355-y
DOI: 10.1007/s10858-005-3355-y
Altmetrics provided by Altmetric
