Folding of the nascent peptide chain into a biologically active protein.
Folding of the nascent peptide chain into a biologically active protein.
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DOI：
10.1021/bi00406a001
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发表时间：
1988-03
期刊：
影响因子：
2.9
通讯作者：
C. Tsou
中科院分区：
文献类型：
--
作者：
C. Tsou
具有完整序列的变性蛋白质的重折叠可能不够快，无法解释生物合成过程中生长的肽链的体内折叠。由于一些肽片段的二级结构与完整分子中相应片段的二级结构没有什么不同，并且一些蛋白质的天然二硫键可以共价形成，因此建议新生链的折叠在合成期间早期开始。然而，在链延伸期间和在完整的肽链的翻译后修饰之后可能需要进一步的调整以产生生物活性蛋白质的天然构象。
The refolding of denatured proteins with complete sequences may not be fast enough to account for the in vivo folding of growing peptide chains during biosynthesis. As some peptide fragments have secondary structures not unlike those of the corresponding segments in the intact molecules and native disulfide bonds of some proteins can form cotranslationally, it is suggested that the folding of the nascent chain begins early during synthesis. However, further adjustments may be necessary during chain elongation and after posttranslational modifications of the completed peptide chain to generate the native conformation of a biologically active protein.