Spectral density mapping protocols for analysis of molecular motions in disordered proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00073529" target="_blank" >RIV/00216224:14740/14:00073529 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/14:00439577

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs10858-014-9816-4" target="_blank" >http://link.springer.com/article/10.1007%2Fs10858-014-9816-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10858-014-9816-4" target="_blank" >10.1007/s10858-014-9816-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Spectral density mapping protocols for analysis of molecular motions in disordered proteins

Popis výsledku v původním jazyce

Spectral density mapping represents the method of choice for investigations of molecular motions of intrinsically disordered proteins (IDPs). However, the current methodology has been developed for well-folded proteins. In order to find conditions for areliable analysis of relaxation of IDPs, accuracy of the current reduced spectral density mapping protocols applied to IDPs was examined and new spectral density mapping methods employing cross-correlated relaxation rates have been designed. Various sources of possible systematic errors were analyzed theoretically and the presented approaches were tested on a partially disordered protein, delta subunit of bacterial RNA polymerase. Results showed that the proposed protocols provide unbiased description of molecular motions of IDPs and allow to separate slow exchange from fast dynamics.

Název v anglickém jazyce

Spectral density mapping protocols for analysis of molecular motions in disordered proteins

Popis výsledku anglicky

Spectral density mapping represents the method of choice for investigations of molecular motions of intrinsically disordered proteins (IDPs). However, the current methodology has been developed for well-folded proteins. In order to find conditions for areliable analysis of relaxation of IDPs, accuracy of the current reduced spectral density mapping protocols applied to IDPs was examined and new spectral density mapping methods employing cross-correlated relaxation rates have been designed. Various sources of possible systematic errors were analyzed theoretically and the presented approaches were tested on a partially disordered protein, delta subunit of bacterial RNA polymerase. Results showed that the proposed protocols provide unbiased description of molecular motions of IDPs and allow to separate slow exchange from fast dynamics.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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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)

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Biomolecular NMR

ISSN

0925-2738

e-ISSN

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Svazek periodika

58

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

15

Strana od-do

193-207

Kód UT WoS článku

000332743800005

EID výsledku v databázi Scopus

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