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

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Publikace nespadá pod Lékařskou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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KADEŘÁVEK Pavel ZAPLETAL Vojtěch RABATINOVÁ Alžběta KRÁSNÝ Libor SKLENÁŘ Vladimír ŽÍDEK Lukáš

Rok publikování 2014
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Biomolecular NMR
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www http://link.springer.com/article/10.1007%2Fs10858-014-9816-4
Doi http://dx.doi.org/10.1007/s10858-014-9816-4
Obor Biochemie
Klíčová slova Nuclear magnecit resonance; Relaxation; Spectral density function; Intrinsically disordered proteins
Popis 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 a reliable 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.
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