Backbone Motions of Free and Pheromone-Bound Major Urinary Protein I Studied by Molecular Dynamics Simulation

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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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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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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)

Rok uplatnění

2007

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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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