Broglia R A, Tiana G
Dipartimento di Fisica, Universitá di Milano and INFN, sezione di Milano, via Celoria 16, 20133 Milano, Italy.
J Biol Phys. 2001 Jun;27(2-3):161-8. doi: 10.1023/A:1013185829193.
Through systematic studies of lattice Monte Carlo simulations of thefolding of designed heteropolymers, we have identified a hierarchy ofspecific elementary phenomena which control the way single domain proteinfold: a) formation of few, local elementary structures, b) creation ofthe (post-critical) folding nucleus through the assemblage together ofthe local elementary structures, c) relaxation of the remaining aminoacids to the native conformation. These results, which are consistentwith a two-state kinetics of the folding of small, single domain proteins,where the local elementary structures and the folding nucleus can be viewedas hidden intermediates along the reaction pathway, provide the basis fora strategy to read the tertiary structure of a protein from its aminoacid sequence.
通过对设计的杂聚物折叠的晶格蒙特卡罗模拟进行系统研究，我们确定了一系列特定的基本现象，这些现象控制着单结构域蛋白质的折叠方式：a）形成少数局部基本结构；b）通过将局部基本结构聚集在一起形成（临界后）折叠核；c）其余氨基酸弛豫至天然构象。这些结果与小的单结构域蛋白质折叠的两态动力学一致，其中局部基本结构和折叠核可被视为反应途径上的隐藏中间体，为从氨基酸序列读取蛋白质三级结构的策略提供了基础。
