Abstract
Many membrane remodelling pathways involve the process of smaller protein units organizing into higher order structures with defined functional roles. This self-assembly is governed by the stability of protein-protein and protein-membrane interactions. However, the extent to which the thermodynamics of these interactions are affected by membrane localization has received limited study. Previously, our lab has quantified how localization to the 2D membrane surface, by reducing the search space, can dramatically enhance and accelerate dimerization.
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