Kay M S, Baldwin R L
Department of Biochemistry, Stanford University Medical Center, California 94305-5307, USA.
Nat Struct Biol. 1996 May;3(5):439-45. doi: 10.1038/nsb0596-439.
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.
通过圆二色性和荧光监测的尿素变性研究了特定堆积对抹香鲸脱辅基肌红蛋白中间体稳定性的贡献。与早期关于pH诱导的去折叠研究得出的结论相反，破坏由A、G和H螺旋形成的亚结构域内天然堆积位点的突变会使中间体不稳定。基于这些结果，有人提出中间体是通过部分形成的类似天然的三级结构以及形成亚结构域折叠中间体的非特异性疏水相互作用来稳定的。这些结果有助于解释中间体如何获得其结构和稳定性。
