کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10768338 | 1050807 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
SMR proteins SugE and EmrE bind ligand with similar affinity and stoichiometry
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Suppressor of a groEL mutation protein E (SugE) is a small multidrug resistance (SMR) homologue. In comparison with other SMR proteins, SugE promotes bacterial resistance to a narrow range of quaternary ammonium compounds (QACs). Isothermal titration calorimetry was used to study the binding of QACs to Escherichia coli SugE in different membrane mimetic environments. In this study, the binding stoichiometry of SugE to drug was found to be 1:1, and the binding of SugE to drug was observed with the dissociation constant (KD) in the micromolar range for each of the drugs in the membrane mimetic environments explored. This interaction appears to be enthalpy-driven with enthalpies of 8-12Â kcal/mol for each of the drugs. These results are similar to those found with drug binding to the SMR protein EmrE in an earlier study.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 335, Issue 1, 16 September 2005, Pages 105-111
Journal: Biochemical and Biophysical Research Communications - Volume 335, Issue 1, 16 September 2005, Pages 105-111
نویسندگان
Curtis W. Sikora, Raymond J. Turner,