Contributions to membrane-embedded-protein diffusion beyond hydrodynamic theories.

The diffusion coefficients of proteins embedded in a lipid membrane are traditionally described by the hydrodynamic Saffman-Delbrück theory, which predicts a weak dependence of the diffusion coefficient on protein radius, D∼lnR. Recent experiments have observed a stronger dependence, D∼1/R. This has led to speculation that the primary sources of drag on the protein are not hydrodynamic, but originate in coupling to other fields, such as lipid chain stretching or tilt. We discuss a generic model of a protein coupled to a nonconserved scalar order parameter (e.g., chain stretching), and show that earlier results may not be as universal as previously believed. In particular, we note that the drag depends on the way the protein-order parameter coupling is imposed. In this model, D∼1/R can be obtained if the protein is much larger than the order parameter correlation length. However, if we modify the model to include advection of the order parameter, which is a more appropriate assumption for a fluid membrane, we find that the entrainment of the order parameter by the protein's motion significantly changes the scaling of the diffusion coefficient. For parameters appropriate to protein diffusion, the Saffman-Delbrück-like scaling is restored, but with an effective radius for the protein that depends on the order parameter's correlation length. This qualitative difference suggests that hydrodynamic effects cannot be neglected in the computation of drag on a protein interacting with the membrane.