Peptide-lipid interactions can be investigated with spin-labelled lipid probes by using electron spin resonance (ESR) methods that have been developed for studying lipid-protein interactions with both integral and peripheral membrane proteins and also with surface-binding proteins that additionally penetrate the membrane. This approach has the advantage that a direct comparison can be made with the databank of ESR results from the various types of membrane protein. The appropriateness of the peptides as models for membrane proteins, or for their specific segments, can then be assessed. Further, differences in behaviour can be readily identified, as for example in the case of surface-active cytolytic or fusogenic peptides. Comparison with thermodynamic predictions for membrane insertion provides a useful adjunct to the spin-label method.
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Conference Article|
August 01 2001
Application of electron spin resonance for investigating peptide-lipid interactions, and correlation with thermodynamics
D. Marsh
D. Marsh
1
1Max-Planck-Institut für biophysikalische Chemie, Abt. Spektroskopie, 37070 Goöttingen, Germany
1e-mail dmarsh@gwdg.de
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Publisher: Portland Press Ltd
Received:
February 20 2001
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2001 Biochemical Society
2001
Biochem Soc Trans (2001) 29 (4): 582–589.
Article history
Received:
February 20 2001
Citation
D. Marsh; Application of electron spin resonance for investigating peptide-lipid interactions, and correlation with thermodynamics. Biochem Soc Trans 1 August 2001; 29 (4): 582–589. doi: https://doi.org/10.1042/bst0290582
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