Informace o publikaci
BACKBONE MOTIONS OF DELTA SUBUNIT OF RNA POLYMERASE FROM BACILLUS SUBTILIS ON VARIOUS TIME SCALES
| Autoři | |
|---|---|
| Rok publikování | 2010 |
| Druh | Konferenční abstrakty |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | Nuclear magnetic resonance is a powerfull tool for the study of molecular motions with atomic resolution. Information about dynamics is important for an understanding biomolecular functions. The current project focuses on inspection of the backbone motions in proteins. The work covers description of the dynamics within the two ranges of timescales which are usually referred as slow (micro-miliseconds) and fast (pico-nanoseconds). The investigation of fast motions is usually based on the measurement of 15N-1H spin pair relaxation rate. The standard process is following. The relaxation experiments R1, R2, NOE are performed at several magnetic field and the appropriate auto and cross relaxation rates are extracted. The measured data are then usually interpreted within the Model Free approach [1][2]. For the purpose of study slow motions the Carr-Purcell-Meiboom-Gill experiment (CPMG) [3][4] may be utilized and it can be accompanied by the data obtained from the measurement of relaxation rates under the condition of continuous irradiation (R1rho) [3]. Compared to the analysis of the fast motion, the interpretation is not so straightforward and overlooking possible complications may corrupt the reliability of the results. The hazard of misinterpretation of the data is discussed. The mentioned methods were applied to investigate the backbone motions in delta-subunit of RNA polymerase from Bacillus subtilis. Only the structured N-terminal domain was studied [5]. The correlation between the conserved residues within the sequence and the residues affected by the structural changes at micro-miliseconds timescale was observed, while the residues undergoing the most extensive fast motion were found in a different part of the molecule. [1] Lipari G., Szabo A., Journal of American Chemical Society, 104, 4546-4559, 1982 [2] Lipari G., Szabo A., Journal of American Chemical Society, 104, 4559-4570, 1982 [3] Palmer A.G., Kroenke C.D., Loria J.P., Methods in Enzymology, 339, 204-238, 2001 [4] Long D., Liu M.L., Yang D.W., Journal of American Chemical Society, 130, 2432-2433, 2008 [5] Motáčková V., et al., Proteins: Structure, Function and Bioinformatics, 2010 (in press) |