Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation.
Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation.
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DOI：
10.1002/pro.3118
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发表时间：
2017-04
期刊：
影响因子：
--
通讯作者：
Wallace BA
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文献类型：
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作者：
Yoneda JS;Miles AJ;Araujo AP;Wallace BA
用同步辐射圆二色光谱法研究了由不同二级结构和折叠类型组成的球状蛋白质，以确定脱水对其二级结构的影响。它们在膜形成过程中去除大量水后仅表现出微小的变化，与先前报道的通过冻干脱水的蛋白质的研究相反（其中检测到螺旋结构的大量损失和片结构的增加）。球状蛋白几乎没有观察到构象变化，这与以相同方式干燥的内在无序蛋白（IDP）形成对比：在溶液中几乎完全无序结构的IDPs，表现出增加的规则（大部分是螺旋）二级结构，表明形成新的蛋白质内氢键取代溶剂蛋白质氢键，在一个过程中，这可能会模拟发生的相互作用时，IDP结合到合作伙伴分子。因此，这项研究表明，球状和内在无序的蛋白质的二级结构表现非常不同的脱水后，和电影是一个潜在的有用的格式检查脱水可溶性蛋白质和评估IDP的结构。
Globular proteins composed of different secondary structures and fold types were examined by synchrotron radiation circular dichroism spectroscopy to determine the effects of dehydration on their secondary structures. They exhibited only minor changes upon removal of bulk water during film formation, contrary to previously reported studies of proteins dehydrated by lyophilization (where substantial loss of helical structure and gain in sheet structure was detected). This near lack of conformational change observed for globular proteins contrasts with intrinsically disordered proteins (IDPs) dried in the same manner: the IDPs, which have almost completely unordered structures in solution, exhibited increased amounts of regular (mostly helical) secondary structures when dehydrated, suggesting formation of new intra‐protein hydrogen bonds replacing solvent‐protein hydrogen bonds, in a process which may mimic interactions that occur when IDPs bind to partner molecules. This study has thus shown that the secondary structures of globular and intrinsically disordered proteins behave very differently upon dehydration, and that films are a potentially useful format for examining dehydrated soluble proteins and assessing IDPs structures.