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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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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2006
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| 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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