The TFE-induced transient native-like structure of the intrinsically disordered \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\varvec\sigma_{ 4}^{ 70}$$\end{document}σ470 domain of Escherichia coli RNA polymerase

• Published in: European biophysics journal 2014-01, Vol.43 (12), p.581-594
• Main Authors: Kaczka, Piotr, Winiewska, Maria, Zhukov, Igor, Rempoła, Bożenna, Bolewska, Krystyna, Łoziński, Tomasz, Ejchart, Andrzej, Poznańska, Anna, Wierzchowski, Kazimierz L., Poznański, Jarosław
• Format: Article
• Language: English
• Subjects: Original Paper
• ISSN: 0175-7571; 1432-1017
• DOI: 10.1007/s00249-014-0987-4

The transient folding of domain 4 of an E. coli RNA polymerase \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\sigma^{70}$$\end{document} σ 70 subunit ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$r{\text{EC}}\sigma_{4}^{70}$$\end{document} r EC σ 4 70 ) induced by an increasing concentration of 2,2,2-trifluoroethanol (TFE) in an aqueous solution was monitored by means of CD and heteronuclear NMR spectroscopy. NMR data, collected at a 30 % TFE, allowed the estimation of the population of a locally folded \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$r{\text{EC}}\sigma_{4}^{70}$$\end{document} r EC σ 4 70 structure (CSI descriptors) and of local backbone dynamics ( 15 N relaxation). The spontaneous organization of the helical regions of the initially unfolded protein into a TFE-induced 3D structure was revealed from structural constraints deduced from 15 N- to 13 C-edited NOESY spectra. In accordance with all the applied criteria, three highly populated α-helical regions, separated by much more flexible fragments, form a transient HLHTH motif resembling those found in PDB structures resolved for homologous proteins. All the data taken together demonstrate that TFE induces a transient native-like structure in the intrinsically disordered protein.