The possible role of electrostatic interactions for membrane binding and pore formation of annexin V has been analysed on the basis of a simple dielectric model. It is suggested that the binding of phospholipids to annexin V is regulated, at least initially, by the protein's electrostatic potential.
An EPR Method for Studying Annexin-Biomembrane Interaction
β Scribed by F.M. Megli; M. Selvaggi; A. Delisi; E. Quagliariello
- Book ID
- 102967567
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 780 KB
- Volume
- 214
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Annexin p34 spin label has been used as a probe for studying annexin-membrane Ca-mediated interaction. The EPR spectrum of the purified probe is able to monitor the binding of the protein to phospholipid vesicles and isolated mitochondrial membranes, with increasing calcium concentration, as revealed by the calculated rotational correlation time. A novel mathematical approach is proposed to provide a direct estimation of annexin percentage binding to membranes, based on the correlation time calculated from experimental EPR spectra.
π SIMILAR VOLUMES
The method described was used to observe quantum oscillations of the surface impedance from large sections of the Fermi surface of tin. The cylindrical specimen was heated inductively by 20 kHz currents. The 'freezing-in' of the specimen in the pressure transmitting medium was carried out at liquid