Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance

Biochemistry ◽  
1992 ◽  
Vol 31 (33) ◽  
pp. 7511-7518 ◽  
Author(s):  
Nicholas J. P. Ryba ◽  
Derek Marsh
Keyword(s):  
Electron Spin Resonance ◽  
Electron Spin ◽  
Protein Interactions ◽  
Rotational Diffusion ◽  
Saturation Transfer ◽  
Bovine Rhodopsin ◽  
Spin Resonance ◽  
Lipid Protein Interactions ◽  
Chain Lengths

scholarly journals Rotational diffusion of mitochondrial ADP/ATP carrier studied by saturation-transfer electron spin resonance

Biochemistry ◽  
1989 ◽  
Vol 28 (1) ◽  
pp. 407-414 ◽  
Author(s):  
Laszlo I. Horvath ◽  
Anton Munding ◽  
Klaus Beyer ◽  
Martin Klingenberg ◽  
Derek Marsh
Keyword(s):  
Electron Spin Resonance ◽  
Electron Spin ◽  
Rotational Diffusion ◽  
Saturation Transfer ◽  
Spin Resonance

Lipid−Protein Interactions with Cardiac Phospholamban Studied by Spin-Label Electron Spin Resonance†

Biochemistry ◽  
2003 ◽  
Vol 42 (17) ◽  
pp. 5151-5158 ◽  
Author(s):  
Ashish Arora ◽  
Ian M. Williamson ◽  
Anthony G. Lee ◽  
Derek Marsh
Keyword(s):  
Electron Spin Resonance ◽  
Electron Spin ◽  
Protein Interactions ◽  
Spin Label ◽  
Spin Resonance ◽  
Lipid Protein Interactions

scholarly journals Application of electron spin resonance for investigating peptide-lipid interactions, and correlation with thermodynamics

2001 ◽  
Vol 29 (4) ◽  
pp. 582-589 ◽  
Author(s):  
D. Marsh
Keyword(s):  
Electron Spin Resonance ◽  
Membrane Proteins ◽  
Electron Spin ◽  
Protein Interactions ◽  
Surface Binding ◽  
Lipid Interactions ◽  
Peripheral Membrane Proteins ◽  
Spin Resonance ◽  
Surface Active ◽  
Lipid Protein Interactions

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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