| KŘÍŽOVÁ, Hana, Lukáš ŽÍDEK, Martin J. STONE, Milos V. NOVOTNY and Vladimír SKLENÁŘ. 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. Journal of Biomolecular NMR. Dordrecht: Kluwer/Escom, 2004, vol. 28, No 4, p. 369-384. ISSN 0925-2738. |
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@article{493134,
author = {Křížová, Hana and Žídek, Lukáš and Stone, Martin J. and Novotny, Milos V. and Sklenář, Vladimír},
article_location = {Dordrecht},
article_number = {4},
keywords = {backbone dynamics; NMR relaxation; spectral density function;temperature dependence},
language = {eng},
issn = {0925-2738},
journal = {Journal of Biomolecular NMR},
title = {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},
volume = {28},
year = {2004}
}
TY - JOUR
ID - 493134
AU - Křížová, Hana - Žídek, Lukáš - Stone, Martin J. - Novotny, Milos V. - Sklenář, Vladimír
PY - 2004
TI - 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
JF - Journal of Biomolecular NMR
VL - 28
IS - 4
SP - 369
EP - 369
PB - Kluwer/Escom
SN - 09252738
KW - backbone dynamics
KW - NMR relaxation
KW - spectral density function;temperature dependence
N2 - 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.
ER -
KŘÍŽOVÁ, Hana, Lukáš ŽÍDEK, Martin J. STONE, Milos V. NOVOTNY and Vladimír SKLENÁŘ. 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. \textit{Journal of Biomolecular NMR}. Dordrecht: Kluwer/Escom, 2004, vol.~28, No~4, p.~369-384. ISSN~0925-2738.
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