Autonomous subdomains in protein folding.
Autonomous subdomains in protein folding.
复制标题
蛋白质折叠中的自主子结构域。
DOI：
10.1002/pro.5560030301
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Carey,J
中科院分区：
文献类型：
--
作者：
Wu,LC;Grandori,R;Carey,J
对天然降压蛋白和马心细胞色素的蛋白水解解剖已被用来推断完整蛋白折叠途径中的一些步骤。对于这两种蛋白质，小片段能够进行自发的非共价缔合，形成具有天然二级和/或三级结构特征的亚结构域，这表明解剖/重组可能是了解折叠中间体结构的一般方法。这种方法的重要性在于它的简单性和潜在的适用性，以研究各种蛋白质的折叠途径。蛋白酶报告的结构和动力学的天然状态，规避需要事先了解折叠中间体的结构。小片段的蛋白质可以非共价结合的观察结果表明，蛋白质折叠可以被看作是一个分子内的“识别”过程。结果表明，大量的信息编码的蛋白质结构和折叠的水平上的亚结构域，和链的连接只有一个很小的作用，在确定折叠。
Proteolytic dissection of nativetrprepressor and horse heart cytochromechas been used to infer some of the steps in the folding pathways of the intact proteins. For both proteins, small fragments are capable of undergoing spontaneous noncovalent association to form subdomains with native‐like secondary and/or tertiary structural features, suggesting that dissection/reassembly may be a general method to gain insight into the structures of folding intermediates. The importance of this approach is its simplicity and potential applicability to studying the folding pathways of a wide range of proteins. The proteases report on the structure and dynamics of the native state, circumventing the need for prior knowledge of the structures of folding intermediates. The observation that small fragments of proteins can associate noncovalently suggests that protein folding can be viewed as an intramolecular “recognition” process. The results imply that substantial information about protein structure and folding is encoded at the level of subdomains, and that chain connectivity has only a minor role in determining the fold.