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. 2009 Oct 16;15:2050–2060.

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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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ITC measurements of Cu²⁺-binding to the mutant G98R αA-crystallin. The upper panel shows isotherms of enthalpic changes in mutant G98R αA-crystallin upon Cu²⁺ binding. The lower panel shows the fitted curve indicating molar heat values as a function of the Cu²⁺ to protein molar ratio. Measurements were made at 30 °C. The binding isotherm of G98R αA-crystallin exhibits the sequential mode of binding with five sets of binding sites: K1=4.98 (±0.3)×10⁵; ΔH1=-9740±326; ΔS1=-6.07; K2=3.22 (±0.2)×10⁵; ΔH2=8853±1480; ΔS2=54.4; K3=9.23 (±0.62)×10⁴; ΔH3=-1.0 (±0.06)×10⁵; ΔS3=-308; K4=7.58 (±0.6)×10⁴; ΔH4=2.012 (±0.13)×10⁵; ΔS4=686; K5=4.0 (±0.3)×10⁵; ΔH5=-1.337 (±0.09)×10⁵; ΔS5=-415.