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. Author manuscript; available in PMC: 2013 Nov 1.
Published in final edited form as: Nat Struct Mol Biol. 2013 Apr 7;20(5):634–640. doi: 10.1038/nsmb.2548

Figure 4. Binding heat capacity changes.

Figure 4

Binding isotherms and enthalpies derived from ITC for (a) GltPhout and (b) GltPhin. Left panels, thermal powers and heats measured at 15 (solid circles and upper insets, respectively) and 35 °C (solid triangles and lower insets, respectively) are shown. The solid lines are the best fits to independent binding sites model. The fitted ΔH in kcal/mol, KD values in nM and n values were, respectively, in (a): −13.5, 154, 1.0 at 15 °C and −19.4, 1278 and 1.1 at 35 °C; and (b): −12.3, 373, 0.7 at 15 °C and −25.2, 540 and 0.8 at 35 °C. Right panels, temperature dependencies of the binding enthalpies for Asp in the presence of: 10 mM Na+ (solid circles), 1 M Na+ (open circles), and 30 mM Na+, 0.6 mM TBA (solid squares). The data were fitted to straight lines with the slopes corresponding to the ΔCps of binding: −297, −131, −171 cal mol−1 K−1, respectively, for GltPhout and −608, −184, −198 cal mol−1 K−1, respectively, for GltPhin.