Determination of the contribution of the myristoyl group and hydrophobic amino acids of recoverin on its dynamics of binding to lipid monolayers.

ABSTRACT: It has been postulated that myristoylation of peripheral proteins would facilitate their binding to membranes. However, the exact involvement of this lipid modification in membrane binding is still a matter of debate. Proteins containing a Ca(2+)-myristoyl switch where the extrusion of their myristoyl group is dependent on calcium binding is best illustrated by the Ca(2+)-binding recoverin, which is present in retinal rod cells. The parameters responsible for the modulation of the membrane binding of recoverin are still largely unknown. This study was thus performed to determine the involvement of different parameters on recoverin membrane binding. We have used surface pressure measurements and PM-IRRAS spectroscopy to monitor the adsorption of myristoylated and nonmyristoylated recoverin

SUBMITTER: Desmeules P 

PROVIDER: S-EPMC1959526 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature