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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 6.

Figure 6

The mutant R100L/G135W has a stable dimeric state. Mutant R100L/G135W protein was expressed, purified, and refolded from inclusion bodies as described in Methods. Folding reactions were quenched by adding 5× SDS gel-loading buffer [45] to a final dilution of 1× SDS gel loading buffer. 50 μl of sample was loaded on a 4-20% acrylamide continous gradient precast gel to resolve the folded and unfolded populations [12]. The populations of folded monomeric (M) and dimeric (D) species, as well as that of the unfolded (U) species remains constant during the course of 30 days as measured by SDS-PAGE separation.