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Energetics of Ligand-induced Conformational Flexibility in the Lactose Permease of Escherichia coli

Isothermal titration calorimetry has been applied to characterize the thermodynamics of ligand binding to wild-type lactose permease (LacY) and a mutant (C154G) that strongly favors an inward facing conformation. The affinity of wild-type or mutant LacY for ligand and the change in free energy (ΔG)...

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Detalhes bibliográficos
Main Authors: Nie, Yiling, Smirnova, Irina, Kasho, Vladimir, Kaback, H. Ronald
Formato: Artigo
Idioma:Inglês
Publicado em: 2006
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2793331/
https://ncbi.nlm.nih.gov/pubmed/17003033
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M607232200
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