Determination of the Contribution of the Myristoyl Group and Hydrophobic Amino Acids of Recoverin on its Dynamics of Binding to Lipid Monolayers

摘要: It has been postulated that myristoylation of peripheral proteins would facilitate their binding to membranes. However, the exact involvement this lipid modification in membrane is still a matter debate. Proteins containing Ca2+-myristoyl switch where extrusion myristoyl group dependent on calcium best illustrated by Ca2+-binding recoverin, which present retinal rod cells. The parameters responsible for modulation recoverin are largely unknown. This study was thus performed determine different binding. We have used surface pressure measurements and PM-IRRAS spectroscopy monitor adsorption myristoylated nonmyristoylated onto phospholipid monolayers presence absence calcium. curves shown hydrophobic residues strongly accelerate In case calcium, alone its much faster monolayer than infrared spectra revealed behave very upon monolayers. Indeed, indicated allows proper orientation organization as well stronger compared recoverin. Simulations allowed us postulate changes conformation becomes hydrated at large extents estimate with respect plane. addition, electrophoresis trypsin-treated zinc or demonstrated but similar extent such ions.