Temperature Dependent Spectral Density Analysis Applied to Monitoring Backbone Dynamics of Major Urinary Protein-I Complexed with the Pheromone 2-sec-Butyl-4,5-dihydrothiazole

Investor logo

Warning

This publication doesn't include Faculty of Economics and Administration. It includes Faculty of Science. Official publication website can be found on muni.cz.
Authors

KŘÍŽOVÁ Hana ŽÍDEK Lukáš STONE Martin J. NOVOTNY Milos V. SKLENÁŘ Vladimír

Year of publication 2004
Type Article in Periodical
Magazine / Source Journal of Biomolecular NMR
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords backbone dynamics; NMR relaxation; spectral density function;temperature dependence
Description Backbone dynamics of mouse major urinary protein I (MUP-I) was studied by 15N NMR relaxation. Data were collected at multiple temperatures for a complex of MUP-I with its natural pheromonal ligand, 2-sec-4,5-dihydrothiazole, and for the free protein. The measured relaxation rates were analyzed using the reduced spectral density mapping. Graphical analysis of the spectral density values provided an unbiased qualitative picture of the internal motions. Varying temperature greatly increased the range of analyzed spectral density values and therefore improved reliability of the analysis. Quantitative parameters describing the dynamics on picosecond to nanosecond time scale were obtained using a novel method of simultaneous data fitting at multiple temperatures. Both methods showed that the backbone flexibility on the fast time scale is slightly increased upon pheromone binding, in accordance with the previously reported results. Zero-frequency spectral density values revealed conformational changes on the microsecond to millisecond time scale. Measurements at different temperatures allowed to monitor temperature depencence of the motional parameters.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.