Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape
Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape
复制标题
DOI：
10.1529/biophysj.105.077982
复制
发表时间：
2006-02-01
影响因子：
3.4
通讯作者：
Rief, M
中科院分区：
文献类型：
--
作者：
Schlierf, M;Rief, M
蛋白质折叠过程被描述为高维能量景观上的扩散。显示下伏能量面细节的实验数据对于理解折叠是必不可少的。到目前为止，在单分子力学展开实验中，已经使用假设力无关过渡态的简化模型来提取这些信息。在这里，我们表明这个所谓的贝尔模型，虽然很好地拟合力速度数据，但无法再现完全展开的力分布。我们表明，通过应用克莱默斯的扩散模型，我们能够重建一个详细的漏斗状曲率的潜在能量景观，并建立与数据完全一致。我们证明，从机械单分子蛋白质展开实验中获得展开能量景观的空间分辨率细节需要超越贝尔模型的模型。
The protein folding process is described as diffusion on a high-dimensional energy landscape. Experimental data showing details of the underlying energy surface are essential to understanding folding. So far in single-molecule mechanical unfolding experiments a simplified model assuming a force-independent transition state has been used to extract such information. Here we show that this so-called Bell model, although fitting well to force velocity data, fails to reproduce full unfolding force distributions. We show that by applying Kramers' diffusion model, we were able to reconstruct a detailed funnel-like curvature of the underlying energy landscape and establish full agreement with the data. We demonstrate that obtaining spatially resolved details of the unfolding energy landscape from mechanical single-molecule protein unfolding experiments requires models that go beyond the Bell model.