Geometry and symmetry presculpt the free-energy landscape of proteins
Geometry and symmetry presculpt the free-energy landscape of proteins
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DOI：
10.1073/pnas.0402525101
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发表时间：
2004-05-25
影响因子：
11.1
通讯作者：
Maritan, A
中科院分区：
文献类型：
--
作者：
Hoang, TX;Trovato, A;Maritan, A
我们提出了一个简单的物理模型，证明了蛋白质的天然状态折叠可以在几何和对称的基础上出现。我们证明了链式分子固有的各向异性，氢键和立体构型的几何和能量限制，以及疏水性足以产生具有广泛最小值的自由能景观，即使对于均聚物也是如此。这些最小值对应于由蛋白质选择的折叠菜单组成的边缘紧凑结构，以容纳它们的天然状态。我们的结果为理解球状蛋白的共同特征提供了一个总体框架。
We present a simple physical model that demonstrates that the native-state folds of proteins can emerge on the basis of considerations of geometry and symmetry. We show that the inherent anisotropy of a chain molecule, the geometrical and energetic constraints placed by the hydrogen bonds and sterics, and hydrophobicity are sufficient to yield a free-energy landscape with broad minima even for a homopolymer. These minima correspond to marginally compact structures comprising the menu of folds that proteins choose from to house their native states in. Our results provide a general framework for understanding the common characteristics of globular proteins.