Temperature as an Extra Dimension in Multidimensional Protein NMR Spectroscopy. Issue 5 (23rd December 2020)

• Record Type: Journal Article
• Authors: Shchukina, Alexandra; Małecki, Paweł; Mateos, Borja; Nowakowski, Michał; Urbańczyk, Mateusz; Kontaxis, Georg; Kasprzak, Paweł; Conrad‐Billroth, Clara; Konrat, Robert; Kazimierczuk, Krzysztof
• Is Part Of: Chemistry. Volume 27:Issue 5(2021)
• Page Start: 1753
• Page End: 1767
• Publication Date: 2020-12-23
• Subjects: multidimensional spectroscopy -- NMR spectroscopy -- protein dynamics -- protein structures -- structure elucidation; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.202003678
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: NMR spectroscopy is a particularly informative method for studying protein structures and dynamics in solution; however, it is also one of the most time‐consuming. Modern approaches to biomolecular NMR spectroscopy are based on lengthy multidimensional experiments, the duration of which grows exponentially with the number of dimensions. The experimental time may even be several days in the case of 3D and 4D spectra. Moreover, the experiment often has to be repeated under several different conditions, for example, to measure the temperature‐dependent effects in a spectrum (temperature coefficients (TCs)). Herein, a new approach that involves joint sampling of indirect evolution times and temperature is proposed. This allows TCs to be measured through 3D spectra in even less time than that needed to acquire a single spectrum by using the conventional approach. Two signal processing methods that are complementary, in terms of sensitivity and resolution, 1) dividing data into overlapping subsets followed by compressed sensing reconstruction, and 2) treating the complete data set with a variant of the Radon transform, are proposed. The temperature‐swept 3D HNCO spectra of two intrinsically disordered proteins, osteopontin and CD44 cytoplasmic tail, show that this new approach makes it possible to determine TCs and their non‐linearities effectively. Non‐linearities, which indicate the presence of a compact state, are particularly interesting. The complete package of data acquisition and processing software for this new approach are provided. Abstract : Time‐saving processing : The rates of temperature‐dependent chemical shift changes help in protein structure analysis. Three‐dimensional experiments to reveal these changes are often lengthy to the extent of being barely feasible. Two specially tailored data processing techniques yield temperature coefficients and their non‐linearities to overcome this limitation.