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Similarity and Difference in the Unfolding of Thermophilic and Mesophilic Cold Shock Proteins Studied by Molecular Dynamics Simulations

机译：分子动力学模拟研究嗜热和中温冷休克蛋白解折叠的相似性和差异

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Molecular dynamics simulations were performed to unfold a homologous pair of thermophilic and mesophilic cold shock proteins at high temperatures. The two proteins differ in just 11 of 66 residues and have very similar structures with a closed five-stranded antiparallel β-barrel. A long flexible loop connects the N-terminal side of the barrel, formed by three strands (β1–β3), with the C-terminal side, formed by two strands (β4–β5). The two proteins were found to follow the same unfolding pathway, but with the thermophilic protein showing much slower unfolding. Unfolding started with the melting of C-terminal strands, leading to exposure of the hydrophobic core. Subsequent melting of β3 and the β-hairpin formed by the first two strands then resulted in unfolding of the whole protein. The slower unfolding of the thermophilic protein could be attributed to ion pair formation of Arg-3 with Glu-46, Glu-21, and the C-terminal. These ion pairs were also found to be important for the difference in folding stability between the pair of proteins. Thus electrostatic interactions appear to play similar roles in the difference in folding stability and kinetics between the pair of proteins.
机译：进行分子动力学模拟以在高温下展开一对嗜热和嗜温冷休克蛋白。这两种蛋白质仅在66个残基中有11个不同，并且具有非常相似的结构，带有封闭的五链反平行β-桶。一个长长的挠性环将由三股链（β1-β3）形成的枪管的N端侧与由两股链（β4-β5）形成的C端侧连接。发现这两种蛋白遵循相同的展开路径，但是嗜热蛋白显示出慢得多的展开。展开从C端链的熔化开始，导致疏水核心暴露。随后由前两条链形成的β3和β-发夹的解链导致整个蛋白质的解折叠。嗜热蛋白的缓慢展开可能归因于具有Glu-46，Glu-21和C末端的Arg-3的离子对形成。还发现这些离子对对于蛋白质对之间折叠稳定性的差异很重要。因此，静电相互作用似乎在一对蛋白质之间的折叠稳定性和动力学差异中起着相似的作用。

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