کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1388365 | 982788 | 2009 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of the interaction between 2â²-deoxyuridine and human serum albumin
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The binding of 2â²-deoxyuridine to human serum albumin (HSA) was investigated by fluorescence spectroscopy in combination with molecular modeling under simulation of physiological conditions. The quenching mechanism was suggested to be static according to the fluorescence measurement. The thermodynamic parameters: enthalpy change (ÎH) and entropy change (ÎS) were calculated to be â18.87 kJ/mol and 24.00 J/(mol K) according to the Vant'Hoff equation. These data suggest that hydrophobic interactions are the predominant intermolecular forces stabilizing the complex. Experimental results are in agreement with the results obtained by molecular modeling study. In addition, the effects of common ions on the binding constants were also studied at room temperature.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Carbohydrate Research - Volume 344, Issue 5, 31 March 2009, Pages 642-647
Journal: Carbohydrate Research - Volume 344, Issue 5, 31 March 2009, Pages 642-647
نویسندگان
Fengling Cui, Yinghua Yan, Qiangzhai Zhang, Juan Du, Xiaojun Yao, Guirong Qu, Yan Lu,