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Striking stabilization of Arc repressor by an engineered disulfide bond

机译：通过工程二硫键达到稳定电弧抑制器的目的

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A solvent-exposed Cys11-Cys11' disulfide bond was designed to link the antiparallel strands of the beta sheet both in the Arc repressor dimer and in a single-chain variant in which the Arc subunits are connected by a 15-residue peptide tether. In both proteins, the presence of the disulfide bond increased the T-m by approximately 40 degrees C. In the single-chain background, the disulfide bond stabilized Are by 8.5 kcal/mol relative to the reduced form, a significantly larger degree of stabilization than caused by other engineered disulfides and most natural disulfides. This exceptional stabilization arises from a modest effective concentration of the Cys11-Cys11' disulfide in the native state (71 M) and an anomalously low effective concentration in the denatured state (40 mu M). Disulfide cross-linking of the two beta strands in the single-chain Arc background accelerated refolding by a factor of 170 into the sub-microsecond time scale. However, the major energetic effect of the disulfide occurs after the transition state for Arc refolding, slowing unfolding by 200 000-fold. [References: 47]
机译：暴露于溶剂的Cys11-Cys11'二硫键被设计为在Arc阻遏物二聚体和单链变体中连接β片的反平行链，在该单链变体中，Arc亚基通过15个残基的肽链连接。在两种蛋白质中，二硫键的存在都会使Tm升高约40摄氏度。在单链背景下，相对于还原形式，二硫键稳定化后的Are含量为8.5 kcal / mol，其稳定程度远大于其还原形式。其他工程二硫化物和大多数天然二硫化物。这种出色的稳定性是由于天然状态的Cys11-Cys11'二硫化物的有效浓度适中（变性）和变性状态的有效浓度（40μM）异常低。单链弧形背景中两条β链的二硫键交联将亚微秒级的重折叠速度提高了170倍。但是，二硫键的主要能量作用发生在电弧重新折叠的过渡态之后，展开速度降低了20万倍。 [参考：47]

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