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

J 2014

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

KADEŘÁVEK, Pavel, Vojtěch ZAPLETAL, Alžběta RABATINOVÁ, Libor KRÁSNÝ, Vladimír SKLENÁŘ et. al.

Základní údaje

Originální název

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

Autoři

KADEŘÁVEK, Pavel (203 Česká republika, domácí), Vojtěch ZAPLETAL (203 Česká republika, domácí), Alžběta RABATINOVÁ (203 Česká republika), Libor KRÁSNÝ (203 Česká republika), Vladimír SKLENÁŘ (203 Česká republika, domácí) a Lukáš ŽÍDEK (203 Česká republika, garant, domácí)

Vydání

Journal of Biomolecular NMR, Dordrecht, Springer, 2014, 0925-2738

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.141

Kód RIV

RIV/00216224:14740/14:00073529

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1007/s10858-014-9816-4

UT WoS

000332743800005

Klíčová slova anglicky

Nuclear magnecit resonance; Relaxation; Spectral density function; Intrinsically disordered proteins

Štítky

kontrola MP, ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 10. 3. 2015 18:44, Martina Prášilová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GA13-16842S, projekt VaV

Název: PODJEDNOTKY URČUJÍCÍ DNA SPECIFICITU BAKTERIÁLNÍ RNA POLYMERÁZY S FLEXIBILNÍMI DOMÉNAMI: FUNKCE A DYNAMIKA

Investor: Grantová agentura ČR, Podjednotky urcující DNA specificitu bakteriální RNA polymerázy s flexibilními doménami: funkce a dynamika

261863, interní kód MU

Název: BioNMR Facilities - Bio NMR (Akronym: BioNMR)

Investor: Evropská unie, BioNMR Facilities - Bio NMR, Kapacity

Citovat

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.

@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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