期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2008
卷号：105
期号：37
页码：13865-13870
DOI：10.1073/pnas.0804512105
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Multidomain proteins are ubiquitous in both prokaryotic and eukaryotic proteomes. Study on protein folding, however, has concentrated more on the isolated single domains of proteins, and there have been relatively few systematic studies on the effects of domain-domain interactions on folding. We here discuss this issue by examining human {gamma}D-crystallin, spore coat protein S, and a tandem array of the R16 and R17 domains of spectrin as example proteins by using a structure-based model of folding. The calculated results consistently explain the experimental data on folding pathways and effects of mutational perturbations, supporting the view that the connectivity of two domains and the distribution of domain-domain interactions in the native conformation are factors to determine kinetic and equilibrium properties of cooperative folding.
关键词：energy landscape theory ; structure-based model ; circular permutation
