| KADEŘÁVEK, Pavel, Vojtěch ZAPLETAL, Alžběta RABATINOVÁ, Libor KRÁSNÝ, Vladimír SKLENÁŘ a Lukáš ŽÍDEK. Spectral density mapping protocols for analysis of molecular motions in disordered proteins. Journal of Biomolecular NMR. Dordrecht: Springer, 2014, roč. 58, č. 3, s. 193-207. ISSN 0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-014-9816-4. |
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@article{1169199,
author = {Kadeřávek, Pavel and Zapletal, Vojtěch and Rabatinová, Alžběta and Krásný, Libor and Sklenář, Vladimír and Žídek, Lukáš},
article_location = {Dordrecht},
article_number = {3},
doi = {http://dx.doi.org/10.1007/s10858-014-9816-4},
keywords = {Nuclear magnecit resonance; Relaxation; Spectral density function; Intrinsically disordered proteins},
language = {eng},
issn = {0925-2738},
journal = {Journal of Biomolecular NMR},
title = {Spectral density mapping protocols for analysis of molecular motions in disordered proteins},
url = {http://link.springer.com/article/10.1007%2Fs10858-014-9816-4},
volume = {58},
year = {2014}
}
TY - JOUR
ID - 1169199
AU - Kadeřávek, Pavel - Zapletal, Vojtěch - Rabatinová, Alžběta - Krásný, Libor - Sklenář, Vladimír - Žídek, Lukáš
PY - 2014
TI - Spectral density mapping protocols for analysis of molecular motions in disordered proteins
JF - Journal of Biomolecular NMR
VL - 58
IS - 3
SP - 193-207
EP - 193-207
PB - Springer
SN - 09252738
KW - Nuclear magnecit resonance
KW - Relaxation
KW - Spectral density function
KW - Intrinsically disordered proteins
UR - http://link.springer.com/article/10.1007%2Fs10858-014-9816-4
L2 - http://link.springer.com/article/10.1007%2Fs10858-014-9816-4
N2 - 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.
ER -
KADEŘÁVEK, Pavel, Vojtěch ZAPLETAL, Alžběta RABATINOVÁ, Libor KRÁSNÝ, Vladimír SKLENÁŘ a Lukáš ŽÍDEK. Spectral density mapping protocols for analysis of molecular motions in disordered proteins. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer, 2014, roč.~58, č.~3, s.~193-207. ISSN~0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-014-9816-4.
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