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. Author manuscript; available in PMC: 2014 Dec 23.
Published in final edited form as: Biochemistry. 2013 Dec 10;52(51):9347–9357. doi: 10.1021/bi401014k

Figure 4. Sensitivity of rat and human L-FABP secondary structure to temperature induced unfolding.

Figure 4

CD spectra and secondary structure analysis of rat and human L-FABPs were determined as a function of sample temperature as described in Methods. Panels A, C, E, and G show the amount of rat L-FABP total α-helix, total β-sheet, turn, and unordered secondary structure, respectively, as a percentage of the total secondary structure. Panels B, D, F. and H show the amount of human T94T WT L-FABP (●) or human T94A variant L-FABP (○) total α-helix, total β-sheet, turn, and unordered secondary structure, respectively, as a percentage of the total secondary structure. *, P < 0.05 for T94A vs T94T; ***, P < 0.001 for T94A vs T94T.