. Author manuscript; available in PMC: 2010 Mar 31.

Published in final edited form as: Biochemistry. 2009 Mar 31;48(12):2788–2798. doi: 10.1021/bi8019959

Table 1.

Summary of the thermodynamic properties of S100A6, S100A10, and S100A11 binding to AnI and AnII determined using Trp fluorescence titrations and ITC experiments as well as the comparison with structure-based calculations

Protein	AnI K_d (μM)	AnII K_d1 and K_d2 (μM)	AnI ΔC_p,exp kJ/(mol·K)	AnI ΔC_p,calc kJ/(mol·K)	AnII ΔC_p,exp kJ/(mol·K)	AnII ΔC_p,calc kJ/(mol·K)
S100A6	13±4 (17±4)^a		−1.1±0.3	−1.6±0.5
S100A11	5±2 (5±1)^a		−1.3±0.2	−1.5±0.3
S100A11		1.7±1.2 and 9.2±1.9			−1.1±0.2	−1.4±0.3
S100A10		0.5±0.4 and 0.5±0.3			−2.4±0.3	−1.7±0.3

Values in parentheses were determined using Trp fluorescence