Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains.
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(2+)-activated, membrane-docking C2 domains are described.
Malmberg
Nathan J
NJ
Molecular Biophysics Program and Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215, USA. nathan.malmberg@colorado.edu
Falke
Joseph J
JJ
D000818:Animals; D001436:Bacteriorhodopsins / Q000737:chemistry; D001703:Biophysics / Q000379:methods*; D002118:Calcium / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D006801:Humans; D008055:Lipids / Q000737:chemistry; D008958:Models, Molecular; D008962:Models, Theoretical; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013113:Spin Labels
D008055:Lipids; D013113:Spin Labels; D001436:Bacteriorhodopsins; D002118:Calcium