| Автор | Malmberg, Nathan J. |
| Автор | Falke, Joseph J. |
| Дата выпуска | 2005 |
| dc.description | ▪ Abstract Despite the central importance of peripheral membrane proteins to cellular signaling and metabolic pathways, the structures of protein-membrane interfaces remain largely inaccessible to high-resolution structural methods. In recent years a number of laboratories have contributed to the development of an electron paramagnetic resonance (EPR) power saturation approach that utilizes site-directed spin labeling to determine the key geometric parameters of membrane-docked proteins, including their penetration depths and angular orientations relative to the membrane surface. Representative applications to Ca<sup>2+</sup>-activated, membrane-docking C2 domains are described. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | USE OF EPR POWER SATURATION TO ANALYZE THE MEMBRANE-DOCKING GEOMETRIES OF PERIPHERAL PROTEINS: Applications to C2 Domains |
| DOI | 10.1146/annurev.biophys.34.040204.144534 |
| Print ISSN | 1056-8700 |
| Журнал | Annual Review of Biophysics and Biomolecular Structure |
| Том | 34 |
| Первая страница | 71 |
| Последняя страница | 90 |
| Аффилиация | Malmberg, Nathan J.; Molecular Biophysics Program and Department of Chemistry & Biochemistry, University of Colorado, Boulder, Colorado 80309-0215; email: falke@colorado.edu ; nathan.malmberg@colorado.edu |
