BIOTIN CARBOXY TERMINAL DOMAIN FOLDING CALORIMETRY E COLI ACETYL COA CARBOXYLASE

在生物素依赖的羧基酶中，生物素部分是共价的 与生物素羧基载体(BCC)官能团结合 酶通过酰胺键连接到单一的 赖氨酸残留物。在大肠杆菌乙酰辅酶A羧基酶中，bcc 功能存在于一个单独的17kD亚基中。87%的残留物 该亚基的C-末端结构域片段(BCCP87)已显示为 在酶催化下表现出与完整蛋白质相同的行为 生物化反应。远地和远地天体的高分辨率结构 全息形式的域名是可用的。的折叠性 用差示扫描法研究BCCP87的脱氧核糖核酸和全息核糖核酸 量热法，以确定是否有贡献，如果有 平移后对体系热力学稳定性的修饰 蛋白。热力学研究的结果将与 可用结构数据来确定任何 在折叠的能量学上测量到的差异。

In biotin-dependent carboxylases, the biotin moiety is covalently bonded to the Biotin Carboxyl Carrier (BCC) functionality of the enzyme via an amide linkage to the epsilon amino group of a single lysine residue. In E. coli acetyl-CoA carboxylase, the BCC functionality resides in a separate 17 kD subunit. An 87 residue C-terminal domain fragment (BCCP87) of this subunit has been shown to behave identically to the intact protein in the enzyme-catalyzed biotination reaction. High resolution structures of both the apo- and holo-forms of the domain are available. The folding properties of the apo- and holo-forms of BCCP87 will be studied by differential scanning calorimetry to determine the contribution, if any, of a post-translational modification to the thermodynamic stability of the protein. Results of the thermodynamic studies will be combined with the available structural data to determine the structural basis of any measured differences in the energetics of folding.