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. 2017 Oct 26;7:14089. doi: 10.1038/s41598-017-14372-2

Table 1.

Thermodynamic parameters of lactate binding to TlpC LBD and its variants derived from ITC measurements.

Protein K D Enthalpy, ∆H (cal/mol) Entropy, ∆S (cal/mol/degree)
TlpC LBD native 155.0 ± 5.0 µM −21,323.3 ± 713.0 −54.1 ± 2.0
TlpC LBD N213A >3,000
TlpC LBD I218A 3.1 ± 0.6 mM −18,145.0 ± 49.0 −49.4 ± 0.2
TlpC LBD Y249A >3,000
TlpC LBD Y285F >3,000
TlpC LBD F202A >3,000
TlpC LBD K223A >3,000
TlpC LBD S104A 359.0 ± 3.0 µM −13,105 ± 318.0 −28.2 ± 1.0
TlpC LBD Y151A 278.5 ± 2.0 µM −12,040 ± 250.2 −24.1 ± 1.0
TlpC LBD K153A 467.2 ± 5.0 µM −12,730 ± 345.0 −27.5 ± 1.0