Self-assembly of protein monomers into distinct membrane protein oligomers
provides a general mechanism for diversity in the molecular architectures, and
resulting biological functions, of membrane proteins. We develop a general
physical framework describing the thermodynamic competition between different
oligomeric states of membrane proteins. Using the mechanosensitive channel of
large conductance as a model system, we show how the dominant oligomeric states
of membrane proteins emerge from the interplay of protein concentration in the
cell membrane, protein-induced lipid bilayer deformations, and direct
monomer-monomer interactions. Our results suggest general physical mechanisms
and principles underlying regulation of protein function via control of
membrane protein oligomeric state.Comment: 7 pages, 5 figure
