Accurate measurements of the association and dissociation kinetics of myristoylated and unmyristoylated forms of MARCKS-related protein using optical waveguide lightmode spectroscopy (OWLS) reveal that the enhanced association of the myristoylated form is due principally to myristoylation inducing the 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 the shielding of the myristoyl moiety from unfavorable aqueous solvation.