脱辅基细胞色素b5解折叠的热力学
Thermodynamics of apocytochrome b5 unfolding.
作者信息
Pfeil W
机构信息
Max-Delbrück-Center for Molecular Medicine, Berlin-Buch, Germany.
出版信息
Protein Sci. 1993 Sep;2(9):1497-501. doi: 10.1002/pro.5560020914.
Abstract
Apocytochrome b5 from rabbit liver was studied by scanning calorimetry, limited proteolysis, circular dichroism, second derivative spectroscopy, and size exclusion chromatography. The protein is able to undergo a reversible two-state thermal transition. However, transition temperature, denaturational enthalpy, and heat capacity change are reduced compared with the holoprotein. Apocytochrome b5 stability in terms of Gibbs energy change at protein unfolding (delta G) amounts to delta G = 7 +/- 1 kJ/mol at 25 degrees C (pH 7.4) compared with delta G = 25 kJ/mol for the holoprotein. Apocytochrome b5 is a compact, native-like protein. According to the spectral data, the cooperative structure is mainly based in the core region formed by residues 1-35 and 79-90. This finding is in full agreement with NMR data (Moore, C.D. & Lecomte, J.T.J., 1993, Biochemistry 32, 199-207).
摘要
采用扫描量热法、有限蛋白酶解、圆二色性、二阶导数光谱法和尺寸排阻色谱法对兔肝脱辅基细胞色素b5进行了研究。该蛋白质能够发生可逆的两态热转变。然而，与全蛋白相比，转变温度、变性焓和热容变化均降低。在25℃（pH 7.4）下，脱辅基细胞色素b5在蛋白质展开时的吉布斯自由能变化（ΔG）为ΔG = 7±1 kJ/mol，而全蛋白的ΔG = 25 kJ/mol。脱辅基细胞色素b5是一种紧密的、类似天然状态的蛋白质。根据光谱数据，协同结构主要基于由1-35位和79-90位残基形成的核心区域。这一发现与核磁共振数据完全一致（Moore, C.D. & Lecomte, J.T.J., 1993, Biochemistry 32, 199-207）。
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