Broglia R A, Tiana G, Pasquali S, Roman H E, Vigezzi E
Dipartimento di Fisica Universita di Milano and Istituto Nazionale di Fisica Nucleare, I-20133 Milan, Italy.
Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12930-3. doi: 10.1073/pnas.95.22.12930.
Protein aggregation is studied by following the simultaneous folding of two designed identical 20-letter amino acid chains within the framework of a lattice model and using Monte Carlo simulations. It is found that protein aggregation is determined by elementary structures (partially folded intermediates) controlled by local contacts among some of the most strongly interacting amino acids and formed at an early stage in the folding process.
通过在晶格模型框架内跟踪两条设计相同的20字母氨基酸链的同时折叠，并使用蒙特卡罗模拟来研究蛋白质聚集。研究发现，蛋白质聚集由基本结构（部分折叠中间体）决定，这些基本结构由一些相互作用最强的氨基酸之间的局部接触所控制，并在折叠过程的早期形成。
