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SHR Neuro Cancer Cardio Lipid Metab Microb
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.
Doi: 10.3390/molecules18077407
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- Leading authors Med Uni Graz
- Wagner-Lichtenegger Gabriel
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- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Antimicrobial Cationic Peptides - analysis
- Bacterial Toxins - analysis
- Calcium-Binding Proteins - analysis
- Cell Membrane - chemistry
- Cell-Penetrating Peptides - analysis
- Magnetic Fields -
- Membrane Proteins - analysis
- Membrane Proteins - chemistry
- Nuclear Magnetic Resonance, Biomolecular - methods
- Peptides - chemistry
- Find related publications in this database (Keywords)
- NMR spectroscopy
- membrane-bound peptides and proteins
- paramagnetic relaxation
- micelle
- dodecylphosphocholine