Chavez Leslie L, Onuchic José N, Clementi Cecilia
Center for Theoretical Biological Physics and Department of Physics, University of California at San Diego, La Jolla, California 92093, USA.
J Am Chem Soc. 2004 Jul 14;126(27):8426-32. doi: 10.1021/ja049510+.
The prediction of protein folding rates and mechanisms is currently of great interest in the protein folding community. A close comparison between theory and experiment in this area is promising to advance our understanding of the physical-chemical principles governing the folding process. The delicate interplay of entropic and energetic/enthalpic factors in the protein free energy regulates the details of this complex reaction. In this article, we propose the use of topological descriptors to quantify the amount of heterogeneity in the configurational entropy contribution to the free energy. We apply the procedure to a set of 16 two-state folding proteins. The results offer a clean and simple theoretical explanation for the experimentally measured folding rates and mechanisms, in terms of the intrinsic entropic roughness along the populated folding routes on the protein free energy landscape.
蛋白质折叠速率和机制的预测目前在蛋白质折叠领域备受关注。该领域理论与实验的紧密比较有望增进我们对控制折叠过程的物理化学原理的理解。蛋白质自由能中熵与能量/焓因素之间微妙的相互作用调节着这一复杂反应的细节。在本文中，我们提出使用拓扑描述符来量化自由能构型熵贡献中的异质性数量。我们将该方法应用于一组16个两态折叠蛋白质。结果从蛋白质自由能景观上占据的折叠路径的内在熵粗糙度方面，为实验测量的折叠速率和机制提供了清晰简单的理论解释。
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