Pedone Emilia, Saviano Michele, Bartolucci Simonetta, Rossi Mosè, Ausili Alessio, Scirè Andrea, Bertoli Enrico, Tanfani Fabio
Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy.
J Proteome Res. 2005 Nov-Dec;4(6):1972-80. doi: 10.1021/pr050152z.
The effect of SDS, pD, and temperature on the structure and stability of the protein disulfide oxidoreductase from Pyrococcus furiosus (PfPDO) was investigated by molecular dynamic (MD) simulations and FT-IR spectroscopy. pD affects the thermostability of alpha-helices and beta-sheets differently, and 0.5% or higher SDS concentration influences the structure significantly. The experiments allowed us to detect a secondary structural reorganization at a definite temperature and pD which may correlate with a high ATPase activity of the protein. The MD simulations supported the infrared data and revealed the different behavior of the N and C terminal segments, as well as of the two active sites.
通过分子动力学（MD）模拟和傅里叶变换红外光谱（FT-IR）研究了十二烷基硫酸钠（SDS）、质子浓度（pD）和温度对嗜热栖热菌蛋白质二硫键氧化还原酶（PfPDO）结构和稳定性的影响。pD对α-螺旋和β-折叠的热稳定性影响不同，0.5%及以上的SDS浓度对结构有显著影响。实验使我们能够检测到在特定温度和pD下的二级结构重组，这可能与该蛋白质的高ATP酶活性相关。MD模拟支持了红外数据，并揭示了N端和C端片段以及两个活性位点的不同行为。
