Electron spin resonance investigations of membrane proteins in erythrocytes in muscle diseases. Duchenne and myotonic muscular dystrophy and congenital myotonia

1977 ◽  
Vol 470 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Allan Butterfield
Keyword(s):  
Electron Spin Resonance ◽  
Muscular Dystrophy ◽  
Membrane Proteins ◽  
Electron Spin ◽  
Muscle Diseases ◽  
Spin Resonance ◽  
Myotonic Muscular Dystrophy

Comparative electron spin resonance study of the erythrocyte membrane in myotonic muscular dystrophy

Biochemistry ◽  
1974 ◽  
Vol 13 (25) ◽  
pp. 5078-5082 ◽  
Author(s):  
D. Allan Butterfield ◽  
Allen D. Roses ◽  
Michael L. Cooper ◽  
Stanley H. Appel ◽  
Donald B. Chesnut
Keyword(s):  
Electron Spin Resonance ◽  
Muscular Dystrophy ◽  
Erythrocyte Membrane ◽  
Electron Spin ◽  
Electron Spin Resonance Study ◽  
Spin Resonance ◽  
Myotonic Muscular Dystrophy ◽  
Comparative Electron ◽  
Spin Resonance Study

Notes: Thermal Lability of Membrane Proteins of Age Separated Erythrocytes as Studied by Electron Spin Resonance Spin Label Technique

1987 ◽  
Vol 42 (11-12) ◽  
pp. 1343-1344 ◽  
Author(s):  
Grzegorz Bartosz ◽  
Gabriele Christ ◽  
Harald Bosse ◽  
Roland Stephan ◽  
Helmut Gärtner
Keyword(s):  
Electron Spin Resonance ◽  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Electron Spin ◽  
Spin Label ◽  
Thermal Denaturation ◽  
Spin Resonance ◽  
Resonance Spin ◽  
First Time ◽  
Erythrocyte Membrane Proteins

Thermal lability of bovine erythrocyte membrane proteins was studied by electron spin resonance using maleimide spin label. The temperature of the sample during measurements could be varied for the first time be­ tween 0 and 60 °C with an accuracy of ± 0.1 °C. Our results show that “old” erythrocyte membrane proteins are less stable against thermal denaturation then “young” cells.

scholarly journals Electron Spin Resonance Studies of Erythrocytes from Patients with Duchenne Muscular Dystrophy

1978 ◽  
Vol 61 (2) ◽  
pp. 251-259 ◽  
Author(s):  
Bunzo Sato ◽  
Koichi Nishikida ◽  
Leo T. Samuels ◽  
Frank H. Tyler
Keyword(s):  
Electron Spin Resonance ◽  
Duchenne Muscular Dystrophy ◽  
Muscular Dystrophy ◽  
Electron Spin ◽  
Spin Resonance

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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