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
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.
Grant support
DC 02418
NIDCD NIH HHS - United States
PubMed
14872128
DOI
10.1023/b:jnmr.0000015404.61574.65
PII: 5256334
Knihovny.cz E-resources
- MeSH
- Magnetic Resonance Spectroscopy MeSH
- Models, Molecular MeSH
- Mice MeSH
- Motion MeSH
- Proteins chemistry MeSH
- Temperature * MeSH
- Protein Structure, Tertiary MeSH
- Thiazoles chemistry MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Names of Substances
- 2-(sec-butyl)-4,5-dihydrothiazole MeSH Browser
- major urinary proteins MeSH Browser
- Proteins MeSH
- Thiazoles MeSH
Backbone dynamics of mouse major urinary protein I (MUP-I) was studied by (15)N 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 dependence of the motional parameters.
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