Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein.
Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein.
复制标题
非二硫键蛋白质折叠和组装途径中的二硫键中间体。
DOI：
10.1038/nsb0697-450
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
King,J
中科院分区：
文献类型：
--
作者：
Robinson,AS;King,J
The trimeric parallel β-coil P22 tailspike contains eight cysteines per chain, but lacks disulphide bonds in the native state, in both the crystalline and solution forms. However, cysteines in a folding intermediate are reactive with thiol blocking reagents, which prevent further productive folding bothin vivoandin vitro. Thein vivorefolding yield was independent of the availability of metal ions, but was sensitive to redox potential. Isolation by nondenaturing gel electrophoresis of the protrimer intermediate, a trimeric folding intermediate that precedes the fully folded trimer in thein vivoandin vitropathways, revealed the presence of interchain disulphide bonds. Incubation of the isolated protrimer with reducing agents generated the native trimer. The formation of β-sheets with interdigitated strands from different subunits in the native trimer may require the transient disulphide bonds for proper alignment. To our knowledge this is the first report of a disulphide bond present in a folding intermediate of a non-disulphide bonded protein.
