Myristoylation-induced compaction of a membrane-binding protein

Accurate measurements of the association and dissociation kinetics of myris toylated and unmyristoylated forms of MARCKS-related protein using optical waveguide lightmode spectroscopy (OWLS) reveal that the enhanced associatio n of the myristoylated form is due principally to myristoylation inducing t he protein to adopt a more compact conformation, allowing enhanced packing at the membrane surface, rather than to markedly different association and/ or dissociation kinetics. The driving force for compaction appears to be th e shielding of the myristoyl moiety from unfavorable aqueous solvation.