Scanning tunnelling microscopy images of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms adsorbed on gold under ambient conditions
Scanning tunnelling microscopy images of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms adsorbed on gold under ambient conditions
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DOI：
10.1143/jjap.41.3916
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发表时间：
2002-06-01
期刊：
影响因子：
--
通讯作者：
Iwasaki, H
中科院分区：
文献类型：
--
作者：
Contera, SA;Okajima, T;Iwasaki, H
利用扫描隧道显微镜（STM）在环境条件下观察到球形节杆菌胺氧化酶以holo和apo形式吸附在Au（111）表面。当单个蛋白质分子吸附在裸露的金表面时，它们会变性。虽然他们保持双重外观。单个蛋白质的原子力显微镜图像在横向上与STM的图像很好地对应，STM电压影响变性蛋白质单元之间的距离：负电压使它们分离，正电压使它们相互连接，无序层和有序层的载脂蛋白和holo蛋白已被STM在分子细节水平上分辨出来。位于层上的单个蛋白质呈现紧凑而独特的二聚体形状。载脂蛋白二聚体看起来比全息二聚体大。
Dimeric Arthrobacter globiformis amine oxidase in the holo and apo forms adsorbed onto a Au (111) surface have been observed by scanning tunnelling microscopy (STM) under ambient conditions. Individual protein molecules denature as they adsorb onto a bare Au surface. although they keep a dual appearance. Tapping atomic force microscopy images of individual proteins correspond well with the STM ones in the lateral direction, STM voltage affects the distance between the units of the denatured proteins: negative voltages separate them while positive one,, get them to-ether, Disordered a well as ordered layers of apo and holo proteins have been resolved by STM at molecular detail level. Individual proteins lying on the layers present a compact and a distinct dimeric shape. apo dimers looking bigger than holo dimers.