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. Author manuscript; available in PMC: 2014 Dec 10.
Published in final edited form as: Biochemistry. 2013 Nov 25;52(49):8843–8854. doi: 10.1021/bi4013462

Figure 2.

Figure 2

Origin of aggregation propensity in CRABP1 is more complex than simple increased fraction of the unfolded protein. A. Aggregation propensity (a fraction of insoluble protein) of different CRABP1 WT* mutants as a function of protein destabilization upon single point mutations (see also Table S1). B. Aggregation cores of different CRABP1 WT* aggregation-prone variants (F71A, I52A and L118V) obtained from E. coli inclusion bodies using DMSO-quenched H/D-exchange experiments and previously reported aggregation cores obtained in vitro using the F71A variant of CRABP1 WT*. (25) C. Aggregation propensity of CRABP1 WT* (red, monitored as a fraction of insoluble protein) and fraction of unfolded CRABP1 WT* (black, monitored by intrinsic tryptophan fluorescence spectroscopy) as a function of urea concentrations.