1,2-Dimyristoyl-sn-glycero-3-phosphoserine

1,2-Dimyristoyl-sn-glycero-3-phosphoserine binds preferentially to myristoylated recoverin in the presence of calcium via electrostatic interactions mediated by the protein's N-terminal cluster of positive charges, with a maximum insertion pressure of 36.7 mN/m^[2].
1,2-Dimyristoyl-sn-glycero-3-phosphoserine exhibits a selectively observed calcium-myristoyl switch of myristoylated recoverin upon binding to its monolayers, with Ca²⁺ increasing the maximum insertion pressure by 49.8% and driving preferential binding with a synergy value of 0.6^[2].
1,2-Dimyristoyl-sn-glycero-3-phosphoserine is specifically bound by myristoylated recoverin in the presence of calcium²⁺ in phospholipid monolayers, regardless of its physical state^[2].
1,2-Dimyristoyl-sn-glycero-3-phosphoserine is slightly penetrated by myristoylated recoverin in the presence of calcium²⁺ into its phospholipid monolayers, rather than binding only at the monolayer's aqueous interface^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.