Carey Jannette, Lindman Stina, Bauer Mikael, Linse Sara
Chemistry Department, Princeton University, NJ 08544-1009, USA.
Protein Sci. 2007 Nov;16(11):2317-33. doi: 10.1110/ps.072985007.
The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone.
蛋白质重构和三维结构域交换现象表明,无论蛋白质由一条还是多条多肽链组成,都能获得高度相似的结构。在本综述中,我们以蛋白质重构为视角,来审视蛋白质对链中断的耐受范围,以及一级结构在蛋白质结构和折叠相关特征(包括环形排列、天然未折叠蛋白、别构作用和淀粉样纤维形成)中的作用。结果表明,在共价主链施加的限制条件下,蛋白质中的非共价相互作用足以确定其结构。