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

0439577 - MBÚ 2015 RIV NL eng J - Journal Article
Kadeřávek, P. - Zapletal, V. - Rabatinová, Alžběta - Krásný, Libor - Sklenář, V. - Žídek, L.
Spectral density mapping protocols for analysis of molecular motions in disordered proteins.
Journal of Biomolecular NMR. Roč. 58, č. 12 (2014), s. 193-207. ISSN 0925-2738. E-ISSN 1573-5001
R&D Projects: GA ČR GA13-16842S
Institutional support: RVO:61388971
Keywords : NMR * CROSS-CORRELATED RELAXATION * N-15 NMR RELAXATION * RNA-POLYMERASE
Subject RIV: EC - Immunology; EE - Microbiology, Virology (MBU-M)
Impact factor: 3.141, year: 2014

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.
Permanent Link: http://hdl.handle.net/11104/0242899