Hurtado-Gómez Estefanía, Barrera Francisco N, Neira José L
Instituto de Biología Molecular y Celular, Edificio Torregaitán, Universidad Miguel Hernández, Avda. del Ferrocarril s/n, 03202, Elche, Alicante, Spain.
Biophys Chem. 2005 Apr 1;115(2-3):229-33. doi: 10.1016/j.bpc.2004.12.032. Epub 2004 Dec 24.
The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS), formed by a cascade of several proteins, couples the translocation and phosphorylation of specific sugars across cell membranes. The structure and thermal stability of the first protein (enzyme I, EI) of the PTS in Streptomyces coelicolor is studied by using far-UV circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) at pH 7.0. The deconvolution of FTIR spectra indicates that the protein is mainly composed by a 35% of alpha-helical structure and 30% of beta-sheet. The thermal denaturation curves, as followed by both techniques, show only a midpoint at 330 K. This thermal denaturation behaviour is different to that observed in other members of the EI family.
细菌磷酸烯醇丙酮酸（PEP）：糖磷酸转移酶系统（PTS）由几种蛋白质级联组成，可将特定糖类跨细胞膜的转运与磷酸化偶联起来。利用远紫外圆二色光谱（CD）和傅里叶变换红外光谱（FTIR）在pH 7.0条件下研究了天蓝色链霉菌中PTS的首个蛋白质（酶I，EI）的结构和热稳定性。FTIR光谱的去卷积表明该蛋白质主要由35%的α-螺旋结构和30%的β-折叠组成。两种技术跟踪得到的热变性曲线仅在330 K处有一个中点。这种热变性行为与EI家族其他成员所观察到的不同。
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