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. 2019 Jul 5;117(3):587–601. doi: 10.1016/j.bpj.2019.06.035

Figure 1.

Figure 1

Design of β-clamp mutations to stabilize or destabilize the dimer interface. Monomer A is depicted in gray and Monomer B in purple on the three-dimensional representations. The locations of mutations in Domain 1 (T45 and T47 variants) are depicted with blue beads, while the mutations at the dimer interface (L82D, L82E, L82E I 272A, S107R, and S109R variants) are depicted with green beads on the protein.