Backbone Motions of Free and Pheromone-Bound Major Urinary Protein I Studied by Molecular Dynamics Simulation
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F07%3A00022171" target="_blank" >RIV/00216224:14310/07:00022171 - 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
Backbone Motions of Free and Pheromone-Bound Major Urinary Protein I Studied by Molecular Dynamics Simulation
Popis výsledku v původním jazyce
Molecular motions of free and pheromone-bound mouse major urinary protein~I, previously investigated by NMR relaxation, were simulated in 30-ns molecular dynamics (MD) runs. The backbone flexibility was described in terms of order parameters and correlation times, commonly used in the NMR relaxation analysis. A special attention was paid to the effect of conformational changes on the nanosecond time scale. Time-dependent order parameters were determined in order to separate motions occurring on different time scales. As an alternative approach, slow conformational changes were identified from the backbone torsion angle variances and a "conformationally filtered" order parameters were calculated for well-defined conformation states. A comparison of thedata obtained for the free and pheromone-bound protein showed that some residues are more rigid in the bound form, but larger portion of the protein becomes more flexible upon the pheromone binding. This finding is in a general agreement
Název v anglickém jazyce
Backbone Motions of Free and Pheromone-Bound Major Urinary Protein I Studied by Molecular Dynamics Simulation
Popis výsledku anglicky
Molecular motions of free and pheromone-bound mouse major urinary protein~I, previously investigated by NMR relaxation, were simulated in 30-ns molecular dynamics (MD) runs. The backbone flexibility was described in terms of order parameters and correlation times, commonly used in the NMR relaxation analysis. A special attention was paid to the effect of conformational changes on the nanosecond time scale. Time-dependent order parameters were determined in order to separate motions occurring on different time scales. As an alternative approach, slow conformational changes were identified from the backbone torsion angle variances and a "conformationally filtered" order parameters were calculated for well-defined conformation states. A comparison of thedata obtained for the free and pheromone-bound protein showed that some residues are more rigid in the bound form, but larger portion of the protein becomes more flexible upon the pheromone binding. This finding is in a general agreement
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
BO - Biofyzika
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/LC06030" target="_blank" >LC06030: Biomolekulární centrum</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2007
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 Physical Chemistry B
ISSN
1089-5639
e-ISSN
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Svazek periodika
111
Číslo periodika v rámci svazku
20
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
9
Strana od-do
5731-5739
Kód UT WoS článku
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EID výsledku v databázi Scopus
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