Packing interactions in the apomyglobin folding intermediate
Packing interactions in the apomyglobin folding intermediate
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DOI：
10.1038/nsb0596-439
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发表时间：
1996-05-01
期刊：
影响因子：
--
通讯作者：
Baldwin, RL
中科院分区：
文献类型：
--
作者：
Kay, MS;Baldwin, RL
通过圆二色性和荧光监测尿素变性，研究了特定包装对抹香鲸无肌红蛋白中间体稳定性的贡献。突变破坏了由A、G和H螺旋形成的亚结构域内的天然包装位点，使中间体不稳定，这与早期ph诱导展开的研究得出的结论相反。基于这些结果，中间体被认为是由部分形成的原生三级相互作用和形成亚结构域折叠中间体的非特异性疏水相互作用稳定的。结果有助于解释中间体如何获得其结构和稳定性。
The contribution of specific packing to the stability of the sperm whale apomyoglobin intermediate has been studied by urea denaturation monitored by circular dichroism and fluorescence. Mutations disrupting native packing sites within the subdomain formed by the A, G and H helices destabilize the intermediate, in contrast to the conclusion drawn from earlier studies of pH-induced unfolding. Based on these results, the intermediate is proposed to be stabilized by both partially formed native-like tertiary, and non-specific hydrophobic interactions forming a subdomain folding intermediate. The results help to explain how the intermediate acquires its structure and stability.