Reversible denaturation of the gene V protein of bacteriophage f1.
Reversible denaturation of the gene V protein of bacteriophage f1.
复制标题
噬菌体 f1 基因 V 蛋白的可逆变性。
DOI：
10.1021/bi00225a006
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Terwilliger,TC
中科院分区：
文献类型：
--
作者：
Liang,H;Terwilliger,TC
盐酸胍（GuHCl）诱导的噬菌体f1的基因V蛋白质的变性已经被研究，使用半胱氨酸残基的化学反应性，该半胱氨酸残基被掩埋在折叠的蛋白质中，并且在211和229 nm处的圆二色性（CD）作为折叠形式中的多肽链的分数的测量。据发现，这种二聚体蛋白展开在一个单一的合作过渡从折叠的二聚体到两个未折叠的单体。一个折叠的，单体形式的基因V蛋白在平衡时没有检测到。基因V蛋白在3 M GuHCl中展开和在2 M GuHCl中再折叠的动力学也与折叠的二聚体和两个未折叠的单体之间的过渡一致。盐酸胍浓度依赖性的折叠和展开的速率表明，折叠的过渡态是附近的折叠构象。
The guanidine hydrochloride (GuHCl)-induced denaturation of the gene V protein of bacteriophage fl has been studied, using the chemical reactivity of a cysteine residue that is buried in the folded protein and the circular dichroism (CD) at 211 and 229 nm as measures of the fraction of polypeptidechains in the folded form. It is found that this dimeric protein unfolds in a single cooperative transition from a folded dimer to two unfolded monomers. A folded, monomeric form of the gene V protein was not detected at equilibrium. The kinetics of unfolding of the gene V protein in 3 M GuHCl and the refolding in 2 M GuHCl are also consistent with a transition between a folded dimer and two unfolded monomers. The GuHCl concentration dependence of the rates of folding and unfolding suggests that the transition State for folding is near the folded conformation.