Lateral diffusion of M-13 coat protein in model membranes

Abstract
A fluorescent derivative of the M-13 phage coat protein (MW 5260) was reconstituted into oriented multilayers and giant liposomes of dimyristoylphosphatidylcholine. The rate of lateral diffusion of the labeled protein in the fluid phase was measured as a function of temperature and was comparable to that of lipid probes. The protein had a nonuniform lateral distribution in the solid phase of both types of model membranes. Cardiolipin (0.5 mol %) included in the multilayers had no substantial effect on the diffusion rate.