Understanding β-hairpin formation
Understanding β-hairpin formation
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DOI：
10.1073/pnas.96.16.9068
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发表时间：
1999-08-03
影响因子：
11.1
通讯作者：
Karplus, M
中科院分区：
文献类型：
--
作者：
Dinner, AR;Lazaridis, T;Karplus, M
蛋白质结构基序形成的动力学（例如，α-螺旋和β-发夹）可以提供有关蛋白质折叠早期事件的信息。最近的一项研究使用荧光测量来监测16个残基的P-发夹的折叠热力学和动力学。在本文中，我们得到的自由能表面和构象折叠的原子模型的β-发夹从多通道蒙特卡罗模拟。结果表明，折叠过程中的自由能是下坡的崩溃，然后通过重排，形成一个结构与部分的疏水性集群;发夹氢键从部分集群在两个方向上向外传播。这种折叠机制不同于已发表的实验结果的解释，这是基于螺旋线圈型唯象模型。
The kinetics of formation of protein structural motifs (e.g., alpha-helices and beta-hairpins) can provide information about the early events in protein folding. A recent study has used fluorescence measurements to monitor the folding thermodynamics and kinetics of a 16-residue P-hairpin. In the present paper, we obtain the free energy surface and conformations involved in the folding of an atomistic model for the beta-hairpin from multicanonical Monte Carlo simulations. The results suggest that folding proceeds by a collapse that is downhill in free energy, followed by rearrangement to form a structure with part of the hydrophobic cluster; the hairpin hydrogen bonds propagate outwards in both directions from the partial cluster. Such a folding mechanism differs from the published interpretation of the experimental results, which is based on a helix-coil-type phenomenological model.