力致蛋白变性：网络中的裂纹扩展。
Protein unfolding under force: crack propagation in a network.
机构信息
Department of Physics and Center for Biological Physics, Arizona State University, Tempe, Arizona, USA.
出版信息
Biophys J. 2011 Aug 3;101(3):736-44. doi: 10.1016/j.bpj.2011.05.072.
The mechanical unfolding of a set of 12 proteins with diverse topologies is investigated using an all-atom constraint-based model. Proteins are represented as polypeptides cross-linked by hydrogen bonds, salt bridges, and hydrophobic contacts, each modeled as a harmonic inequality constraint capable of supporting a finite load before breaking. Stereochemically acceptable unfolding pathways are generated by minimally overloading the network in an iterative fashion, analogous to crack propagation in solids. By comparing the pathways to those from molecular dynamics simulations and intermediates identified from experiment, it is demonstrated that the dominant unfolding pathways for 9 of the 12 proteins studied are well described by crack propagation in a network.
使用基于约束的全原子模型研究了一组具有不同拓扑结构的 12 种蛋白质的机械展开。蛋白质表示为通过氢键、盐桥和疏水接触交联的多肽，每个氢键、盐桥和疏水接触都建模为一个谐波不等式约束，在断裂之前能够承受有限的载荷。通过以迭代的方式最小化网络的过载来生成立体化学上可接受的展开途径，类似于固体中的裂纹扩展。通过将这些途径与分子动力学模拟和实验中鉴定的中间体进行比较，证明了所研究的 12 种蛋白质中的 9 种的主要展开途径可以很好地用网络中的裂纹扩展来描述。
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