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.

Basic information

Original name

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

Authors

KADEŘÁVEK, Pavel (203 Czech Republic, belonging to the institution), Vojtěch ZAPLETAL (203 Czech Republic, belonging to the institution), Alžběta RABATINOVÁ (203 Czech Republic), Libor KRÁSNÝ (203 Czech Republic), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution) and Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.141

RIV identification code

RIV/00216224:14740/14:00073529

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000332743800005

Keywords in English

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

Abstract

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.

Links

ED1.1.00/02.0068, research and development project

Name: CEITEC - central european institute of technology

GA13-16842S, research and development project

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

Investor: Czech Science Foundation

261863, interní kód MU

Name: BioNMR Facilities - Bio NMR (Acronym: BioNMR)

Investor: European Union, Capacities

Citovat

KADEŘÁVEK, Pavel, Vojtěch ZAPLETAL, Alžběta RABATINOVÁ, Libor KRÁSNÝ, Vladimír SKLENÁŘ and Lukáš ŽÍDEK. Spectral density mapping protocols for analysis of molecular motions in disordered proteins. Journal of Biomolecular NMR. Dordrecht: Springer, 2014, vol. 58, No 3, p. 193-207. ISSN 0925-2738. Available from: 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 and Lukáš ŽÍDEK. Spectral density mapping protocols for analysis of molecular motions in disordered proteins. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer, 2014, vol.~58, No~3, p.~193-207. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-014-9816-4.

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