Thermodynamics of Nanobody Binding to Lactose Permease.

@article{Hariharan2016ThermodynamicsON,
  title={Thermodynamics of Nanobody Binding to Lactose Permease.},
  author={Parameswaran Hariharan and Magnus L. Andersson and Xiaoxu Jiang and Els Pardon and Jan Steyaert and H Ronald Kaback and Lan Guan},
  journal={Biochemistry},
  year={2016},
  volume={55 42},
  pages={5917-5926}
}
Camelid nanobodies (Nbs) raised against the outward-facing conformer of a double-Trp mutant of the lactose permease of Escherichia coli (LacY) stabilize the permease in outward-facing conformations. Isothermal titration calorimetry is applied herein to dissect the binding thermodynamics of two Nbs, one that markedly improves access to the sugar-binding site and another that dramatically increases the affinity for galactoside. The findings presented here show that both enthalpy and entropy… CONTINUE READING
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