کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9573479 | 1388902 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry](/preview/png/9573479.png)
چکیده انگلیسی
The enthalpy change accompanying the reversible acid-induced transition from the native (N) to the molten-globule (MG) state of bovine cytochrome c was directly evaluated by isothermal acid-titration calorimetry (IATC), a new method for evaluating the pH dependence of protein enthalpy. The enthalpy change was 30 kJ/mol at 30 °C, pH 3.54, with 500 mM KCl. The results of the global analysis of the temperature dependence of the excess enthalpy from 20 to 35 °C demonstrated that the N to MG transition is a two-state transition with a small heat capacity change of 1.1 kJ Kâ1 molâ1. The present findings were also indicative of the pH dependence of the enthalpy and the heat capacity of the MG state, â13 kJ molâ1 pHâ1 and â1.0 kJ Kâ1 molâ1 pHâ1, respectively, at 30 °C within a pH range from 2 to 3.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 113, Issue 2, 1 February 2005, Pages 161-168
Journal: Biophysical Chemistry - Volume 113, Issue 2, 1 February 2005, Pages 161-168
نویسندگان
Shigeyoshi Nakamura, Shun-ichi Kidokoro,