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
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00019739" target="_blank" >RIV/00216224:14310/04:00019739 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
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
Popis výsledku v původním jazyce
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. Themeasured 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 conformationa
Název v anglickém jazyce
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
Popis výsledku anglicky
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. Themeasured 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 conformationa
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2004
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Biomolecular NMR
ISSN
0925-2738
e-ISSN
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Svazek periodika
28
Číslo periodika v rámci svazku
4
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
16
Strana od-do
369
Kód UT WoS článku
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EID výsledku v databázi Scopus
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