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. Author manuscript; available in PMC: 2013 Sep 13.
Published in final edited form as: J Mol Biol. 2012 Mar 3;419(0):89–101. doi: 10.1016/j.jmb.2012.02.043

Figure 1.

Figure 1

The energetic contributions of individual residues in the TM domain of OmpF. OmpF exists in a trimeric state, with strands 1-5 and strand 16 forming the interaction surface. Among the 16 strands, strands 1-6 and strand 15-16 are found to have the highest overall energy values based on the empirical potential function TmSIP. These strands largely coincide with the protein-protein interaction interface. a) The empirical energy profile of all residues facing the lipids in strands 1-6 and 15-16. b) Residues R100, G19, G135, and N141 are unstable compared to the rest of the residues. R100 interacts with the loop between strands 3 and 4 from another chain, which is thought a major contributor of interchain interactions [33]. G19, G135 and N141 (not shown) are located in strands 1, 6, and 6 respectively.