Max-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam, Germany.
Biochem Biophys Res Commun. 2012 Jan 6;417(1):122-8. doi: 10.1016/j.bbrc.2011.11.067. Epub 2011 Dec 1.
Circular dichroism (CD) spectroscopy of five Arabidopsis late embryogenesis abundant (LEA) proteins constituting the plant specific families LEA_5 and LEA_6 showed that they are intrinsically disordered in solution and partially fold during drying. Structural predictions were comparable to these results for hydrated LEA_6, but not for LEA_5 proteins. FTIR spectroscopy showed that verbascose, but not sucrose, strongly affected the structure of the dry proteins. The four investigated globular proteins were only mildly affected by drying in the absence, but strongly in the presence of sugars. These data highlight the larger structural flexibility of disordered compared to globular proteins and the impact of sugars on the structure of both disordered and globular proteins during drying.
圆二色性（CD）光谱分析表明，构成植物特异性 LEA_5 和 LEA_6 家族的 5 种拟南芥晚期胚胎丰富（LEA）蛋白在溶液中是固有无序的，并在干燥过程中部分折叠。结构预测与水合 LEA_6 的结果相当，但与 LEA_5 蛋白的结果不同。傅里叶变换红外光谱（FTIR）表明，毛蕊花糖而不是蔗糖强烈影响干燥蛋白的结构。在没有糖的情况下，四种研究的球状蛋白仅受到轻微影响，但在存在糖的情况下，它们受到强烈影响。这些数据突出显示了无序蛋白与球状蛋白相比具有更大的结构灵活性，以及糖对干燥过程中无序和球状蛋白结构的影响。
