蛋白质折叠成全β类和全α类。
Protein folds in the all-beta and all-alpha classes.
作者信息
Chothia C, Hubbard T, Brenner S, Barns H, Murzin A
机构信息
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
出版信息
Annu Rev Biophys Biomol Struct. 1997;26:597-627. doi: 10.1146/annurev.biophys.26.1.597.
Analysis of the structures in the Protein Databank, released in June 1996, shows that the number of different protein folds, i.e. the number of different arrangements of major secondary structures and/or chain topologies, is 327. Of these folds, approximately 25% belong to the all-alpha class, 20% belong to the all-beta class, 30% belong to the alpha/beta class, and 25% belong to the alpha + beta class. We describe the types of folds now known for the all-beta and all-alpha classes, emphasizing those that have been discovered recently. Detailed theories for the physical determinants of the structures of most of these folds now exist, and these are reviewed.
对1996年6月发布的蛋白质数据库中的结构分析表明，不同蛋白质折叠的数量，即主要二级结构和/或链拓扑结构的不同排列数量为327种。在这些折叠中，约25%属于全α类，20%属于全β类，30%属于α/β类，25%属于α + β类。我们描述了目前已知的全β类和全α类折叠的类型，重点介绍了最近发现的那些。现在已经存在关于这些折叠中大多数结构的物理决定因素的详细理论，并对这些理论进行了综述。
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