کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9021505 | 1561374 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The binding of 10 general anesthetics to a four-alpha-helix bundle protein displays enthalpy-entropy compensation
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
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چکیده انگلیسی
Isothermal titration calorimetry has been used to characterize the binding of 10 volatile general anesthetics to the hydrophobic core of a four-α-helix bundle protein. This relatively small protein (124 residues) is able to bind a total of 10 volatile general anesthetics with affinities that approximate their respective EC50 values for the anesthetic state, either in man, or in intact animals. This suggests that the four-α-helix bundle represents a good model for the in vivo central nervous system sites of general anesthetic action. The enthalpy changes associated with anesthetic binding to the four-α-helix bundle correlate well with the entropy changes associated with the binding (r = 0.942). Enthalpy-entropy compensation is consistent with the prediction that stronger binding of the anesthetic results in less mobility and therefore greater losses in configurational entropy.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Congress Series - Volume 1283, November 2005, Pages 219-222
Journal: International Congress Series - Volume 1283, November 2005, Pages 219-222
نویسندگان
Tao Zhang, Jonas S. Johansson,