Tatham A S, Drake A F, Shewry P R
Biochem J. 1985 Mar 1;226(2):557-62. doi: 10.1042/bj2260557.
A combination of c.d. spectroscopy and computer prediction is used to show that C hordein has an unusual secondary structure with an absence of alpha-helix and beta-sheet, but the presence of regularly repeated beta-turns. This is associated with a repetitive primary structure based mainly on blocks of eight residues. Similar spectral changes occurred when the protein was heated from 6 to 86 degrees C in aq. 70% (v/v) ethanol or dissolved in increasing concentrations (50-100%, v/v) of trifluoroethanol in water. The studies indicated that the conformation is stabilized by strong hydrophobic interactions and by extensive hydrogen-bonding.
圆二色光谱法和计算机预测相结合的方法被用于表明大麦醇溶蛋白具有不寻常的二级结构,其缺乏α-螺旋和β-折叠,但存在规则重复的β-转角。这与主要基于八个残基组成的重复一级结构相关。当蛋白质在70%(v/v)乙醇水溶液中从6℃加热到86℃,或溶解于水相中浓度不断增加(50 - 100%,v/v)的三氟乙醇中时,会出现类似的光谱变化。研究表明,该构象通过强烈的疏水相互作用和广泛的氢键作用得以稳定。