Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids
Karsisiotis, Andreas Ioannis, Deacon, Oliver M, Macdonald, Colin, Blumenschein, Tharin MA, Moore, Geoffrey R and Worrall, Jonathan AR (2017) Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids. Biomolecular NMR Assignments, 11 (2). 165–168. ISSN 1874-2718
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Abstract
Human cytochrome c plays a central role in the mitochondrial electron transfer chain and in the intrinsic apoptosis pathway. Through the interaction with the phospholipid cardiolipin, cytochrome c triggers release of pro-apoptotic factors, including itself, from the mitochondrion into the cytosol of cells undergoing apoptosis. The cytochrome c/cardiolipin complex has been extensively studied through various spectroscopies, most recently with high-field solution and solid-state NMR spectroscopies, but there is no agreement between the various studies on key structural features of cytochrome c in its complex with cardiolipin. In the present study, we report backbone 1H, 13C, 15N resonance assignments of acid-denatured human cytochrome c in the aprotic solvent dimethylsulfoxide. These have led to the assignment of a reference 2D 1H-15N HSQC spectrum in which out of the 99 non-proline residues 87% of the backbone amides are assigned. These assignments are being used in an interrupted H/D exchange strategy to map the binding site of cardiolipin on human cytochrome c.
Item Type: | Article |
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Uncontrolled Keywords: | human cytochrome c,apoptosis,cardiolipin,acid-denatured,dmso |
Faculty \ School: | Faculty of Science Faculty of Science > School of Chemistry |
Depositing User: | Pure Connector |
Date Deposited: | 04 Mar 2017 01:41 |
Last Modified: | 06 Nov 2020 01:10 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/62851 |
DOI: | 10.1007/s12104-017-9740-0 |
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