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. Author manuscript; available in PMC: 2012 Oct 21.
Published in final edited form as: J Mol Biol. 2011 Aug 24;413(2):484–494. doi: 10.1016/j.jmb.2011.08.041

Fig. 4.

Fig. 4

At pH 3.8, all remaining hysteresis between the folding and unfolding titrations of OmpLA can be eliminated by avoiding the residual tendency of the protein to aggregate. The excitation wavelength for all fluorescence samples was 295 nm. (A) Updated dilution scheme for titrations of OmpLA that included changes in the protein and guanidine HCl concentrations in the first two dilution steps as compared to Fig. 2A. (B) Wavelength position of maximum fluorescence intensity (λmax) for samples of OmpLA in folding (●) and unfolding (○) titrations with LUVs of DLPC at 37° C and at pH 3.8 after 40 hours. The titrations were prepared according to the scheme in (A). (C) RGD light scattering at 295 nm for the same titrations shown in (B).