Camacho C J, Thirumalai D
Institute for Physical Science and Technology, University of Maryland, College Park 20742.
Proc Natl Acad Sci U S A. 1995 Feb 28;92(5):1277-81. doi: 10.1073/pnas.92.5.1277.
We propose a phenomenological theory that accounts for entropic effects due to loop formation to predict pathways in the kinetics of protein folding. The theory, the basis of which lies in multiple folding pathways and a three-stage kinetics, qualitatively reproduces most of the kinetic measurements in the refolding of bovine pancreatic trypsin inhibitor. The resulting pathways show that nonnative kinetic transients are involved in the productive routes leading to the formation of native intermediates. Our theory emphasizes the importance of the random origin of chain folding initiation structures in directing protein folding.
我们提出了一种现象学理论，该理论考虑了由于环形成而产生的熵效应，以预测蛋白质折叠动力学中的途径。该理论基于多种折叠途径和三阶段动力学，定性地再现了牛胰蛋白酶抑制剂重折叠过程中的大多数动力学测量结果。所得途径表明，非天然动力学瞬态参与了导致天然中间体形成的生产途径。我们的理论强调了链折叠起始结构的随机起源在指导蛋白质折叠中的重要性。
