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

J 2004

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

KŘÍŽOVÁ, Hana; Lukáš ŽÍDEK; Martin J. STONE; Milos V. NOVOTNY; Vladimír SKLENÁŘ et. al.

Základní údaje

Originální název

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

Název česky

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

Autoři

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

Vydání

Journal of Biomolecular NMR, Dordrecht, Kluwer/Escom, 2004, 0925-2738

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.918

Kód RIV

RIV/00216224:14310/04:00019739

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000188853300005

Klíčová slova anglicky

backbone dynamics; NMR relaxation; spectral density function;temperature dependence

Štítky

backbone dynamics, NMR relaxation, spectral density function, temperature dependence

Změněno: 12. 7. 2005 13:02, prof. Mgr. Lukáš Žídek, Ph.D.

Anotace

ORIG CZ

V originále

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.

Česky

Byla měřena dynamika proteinu MUP-I při různých teplotách a navržen způsob grafického vyhodnocení.

Návaznosti

GA203/00/0511, projekt VaV

Název: Studium dynamiky a termodynamiky komplexů myších feromonů s proteiny

Investor: Grantová agentura ČR, Studium dynamiky a termodynamiky komplexů myších feromonů s proteiny

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

Citovat

KŘÍŽOVÁ, Hana; Lukáš ŽÍDEK; Martin J. STONE; Milos V. NOVOTNY a 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, roč. 28, č. 4, s. 369-384. ISSN 0925-2738.

@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 a 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, roč.~28, č.~4, s.~369-384. ISSN~0925-2738.

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