کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9573480 | 1388902 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A calorimetric study on the binding of six general anesthetics to the hydrophobic core of a model protein
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The thermodynamic parameters underlying the binding of six volatile general anesthetics to the hydrophobic core of the four-α-helix bundle (Aα2-L38M)2 are determined using isothermal titration calorimetry. Chloroform, bromoform, trichloroethylene, benzene, desflurane and fluroxene are shown to bind to the four-α-helix bundle with dissociation constants of 880±10, 90±5, 200±10, 900±30, 220±10 and 790±40 μM, respectively. The measured dissociation constants for the binding of the six general anesthetics to the four-α-helix bundle (Aα2-L38M)2 correlate with their human or animal EC50 values. The negative enthalpy changes indicate that favorable polar interactions are achieved between bound anesthetic and the adjacent amino acid side chains. Because of its small size and the ability to bind a variety of general anesthetics, the four-α-helix bundle (Aα2-L38M)2 represents an attractive system for structural studies on anesthetic-protein complexes.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 113, Issue 2, 1 February 2005, Pages 169-174
Journal: Biophysical Chemistry - Volume 113, Issue 2, 1 February 2005, Pages 169-174
نویسندگان
Tao Zhang, Jonas S. Johansson,