Thacher T, Rabitz H
Department of Chemistry, Princeton University, New Jersey 08544.
Biophys J. 1988 Oct;54(4):695-704. doi: 10.1016/S0006-3495(88)83005-4.
A static analysis of bovine pancreatic trypsin inhibitor (BPTI) is presented based on a new discrete/continuum approach to modeling the dynamics of biomolecules. This hybrid method utilizes knowledge of the intramolecular potential and molecular configuration to generate a field of elastic modulus tensors. These tensors, which relate the local stress and strain for each atom in the biomolecule, can be used to judge the local rigidity as well as indicate regions of high stress. Comparing the tensor fields for an unrelaxed and a relaxed configuration, the microscopic structure of BPTI is found to be anisotropic and to have regions of stress even when it is relaxed in the potential field. However, when these fields are averaged over the whole protein or over individual residues the structure becomes more isotropic and the stressed regions vanish. Using these averaged tensors, we calculated bulk properties such as Young's modulus and the Lamé constants and they agreed with previously reported values.
基于一种用于模拟生物分子动力学的新型离散/连续方法，对牛胰蛋白酶抑制剂（BPTI）进行了静态分析。这种混合方法利用分子内势能和分子构型的知识来生成弹性模量张量场。这些张量将生物分子中每个原子的局部应力和应变联系起来，可用于判断局部刚性以及指示高应力区域。比较未松弛构型和松弛构型的张量场，发现BPTI的微观结构是各向异性的，并且即使在势场中松弛时也存在应力区域。然而，当这些场在整个蛋白质或单个残基上进行平均时，结构变得更加各向同性，应力区域消失。使用这些平均张量，我们计算了诸如杨氏模量和拉梅常数等体积性质，它们与先前报道的值一致。
