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

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Authors

KADEŘÁVEK Pavel ZAPLETAL Vojtěch RABATINOVÁ Alžběta KRÁSNÝ Libor SKLENÁŘ Vladimír ŽÍDEK Lukáš

Year of publication 2014
Type Article in Periodical
Magazine / Source Journal of Biomolecular NMR
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://link.springer.com/article/10.1007%2Fs10858-014-9816-4
Doi http://dx.doi.org/10.1007/s10858-014-9816-4
Field Biochemistry
Keywords Nuclear magnecit resonance; Relaxation; Spectral density function; Intrinsically disordered proteins
Description 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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