A test of the ''jigsaw puzzle'' model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
A test of the ''jigsaw puzzle'' model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
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DOI：
10.1073/pnas.93.22.12155
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发表时间：
1996-10-29
影响因子：
11.1
通讯作者：
Matthews, BW
中科院分区：
文献类型：
--
作者：
Gassner, NC;Baase, WA;Matthews, BW
为了测试蛋白质的结构是否以类似于拼图的组装方式确定，在T4溶菌酶的核心内，多达10个相邻残基被蛋氨酸取代。7 -蛋氨酸变体的结构在晶体学上显示与野生型相似，并保持有序的核心。因此，核心残基之间的相互作用不能严格地与拼图碎片的精确空间互补性相比较，相反，在形成核心结构的过程中，一定数量的给予和接受是允许的。一个简化的疏水核心序列，没有遗传选择或基于计算机的设计，足以保留球形蛋白质的天然特性。
To test whether the structure of a protein is determined in a manner akin to the assembly of a jigsaw puzzle, up to 10 adjacent residues within the core of T4 lysozyme were replaced by methionine. Such variants are active and fold cooperatively with progressively reduced stability, The structure of a seven-methionine variant has been shown, crystallographically, to be similar to wild type and to maintain a well ordered core. The interaction between the core residues is, therefore, not strictly comparable with the precise spatial complementarity of the pieces of a jigsaw puzzle, Rather, a certain amount of give and take in forming the core structure is permitted, A simplified hydrophobic core sequence, imposed without genetic selection or computer-based design, is sufficient to retain native properties in a globular protein.