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Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes
Institute of Chemistry/ Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010 Graz, Austria
These authors contributed equally to this work.
* Author to whom correspondence should be addressed.
Received: 26 April 2013; in revised form: 13 June 2013 / Accepted: 20 June 2013 / Published: 25 June 2013
Abstract: Many peptides and proteins are attached to or immersed in a biological membrane. In order to understand their function not only the structure but also their topology in the membrane is important. Solution NMR spectroscopy is one of the most often used approaches to determine the orientation and localization of membrane-bound peptides and proteins. Here we give an application-oriented overview on the use of paramagnetic probes for the investigation of membrane-bound peptides and proteins. The examples discussed range from the large pool of antimicrobial peptides, bacterial toxins, cell penetrating peptides to domains of larger proteins or the calcium regulating protein phospholamban. Topological information is obtained in all these examples by the use of either attached or freely mobile paramagnetic tags. For some examples information obtained from the paramagnetic probes was included in the structure determination.
Keywords: NMR spectroscopy; membrane-bound peptides and proteins; paramagnetic relaxation; micelle; dodecylphosphocholine
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MDPI and ACS Style
Schrank, E.; Wagner, G.E.; Zangger, K. Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes. Molecules 2013, 18, 7407-7435.
Schrank E, Wagner GE, Zangger K. Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes. Molecules. 2013; 18(7):7407-7435.
Schrank, Evelyne; Wagner, Gabriel E.; Zangger, Klaus. 2013. "Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes." Molecules 18, no. 7: 7407-7435.