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首页> 外文期刊>Journal of Molecular Biology >Characterization of the folding kinetics of a three-helix bundle proteinvia a minimalist Langevin model
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Characterization of the folding kinetics of a three-helix bundle proteinvia a minimalist Langevin model

机译：极简朗文模型对三螺旋束蛋白折叠动力学的表征

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摘要

We use a simple off-lattice Langevin model of protein folding to characterize the folding and unfolding of a fast-folding, 46 residue three-helix bundle. Under conditions at which the C-terminal helix is 30% stable, we observe a clear three-state folding mechanism. In the on-pathway intermediate state, the middle and C-terminal helices are folded and in contact with each other, while the N-terminal region remains disordered. Nevertheless, under these conditions this intermediate is thermodynamically unstable relative to its unfolded state. The first and highest folding barrier corresponds to the organization of the hinge between the middle and C-terminal helices. A subsequent major barrier corresponds to the organization of the hinge between the middle and N-terminal helices. Hyperstabilizing the hinge regions leads to twice the folding rate that is obtained from hyperstabilizing the helices, even though much fewer contacts are involved in hinge hyperstabilization than in helix hyperstabilization. Unfolding follows single-exponential kinetics, even at temperatures only slightly above the folding transition temperature.
机译：我们使用蛋白质折叠的简单的非格子Langevin模型来表征快速折叠的46残基三螺旋束的折叠和展开。在C端螺旋稳定30％的条件下，我们观察到清晰的三态折叠机制。在途中的中间状态下，中端和C端螺旋折叠且彼此接触，而N端区域则保持无序。然而，在这些条件下，该中间体相对于其展开状态在热力学上是不稳定的。第一折叠障碍物和最高折叠障碍物对应于中间和C末端螺旋之间的铰链的组织。随后的主要障碍对应于中间和N末端螺旋之间的铰链组织。使铰链区域超稳定导致从超稳定螺旋获得的折叠速率的两倍，即使铰链超稳定涉及的接触比螺旋超稳定少得多。即使在仅稍微高于折叠转变温度的温度下，展开也遵循单指数动力学。

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