Spectral Analysis of a Protein Conformational Switch
Spectral Analysis of a Protein Conformational Switch
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DOI：
10.1103/physrevlett.106.248101
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发表时间：
2011-06-14
影响因子：
8.6
通讯作者：
Rackovsky, S.
中科院分区：
文献类型：
--
作者：
Rackovsky, S.
由单一氨基酸突变引起的蛋白质构象转换的存在，对我们理解蛋白质折叠的物理学提出了一个重要的挑战。通常用于检测结构同源性的序列局部方法无法解释这种现象。我们研究了一组来自链球菌蛋白G的G(A)和G(B)结构域的蛋白质，这些蛋白质因单一残基替换而显示出戏剧性的构象变化。结果表明，这些局部几乎相同的序列可以具有非常不同的全局物理性质模式。这些差异与观察到的构象完全变化是一致的。这些结果表明，用于鉴定结构同源性的序列局部方法可能具有误导性。它们指出了全局序列分析在理解序列-结构关系方面的重要性。
The existence of conformational switching in proteins, induced by single amino acid mutations, presents an important challenge to our understanding of the physics of protein folding. Sequence-local methods, commonly used to detect structural homology, are incapable of accounting for this phenomenon. We examine a set of proteins, derived from the G(A) and G(B) domains of Streptococcus protein G, which are known to show a dramatic conformational change as a result of single-residue replacement. It is shown that these sequences, which are almost identical locally, can have very different global patterns of physical properties. These differences are consistent with the observed complete change in conformation. These results suggest that sequence-local methods for identifying structural homology can be misleading. They point to the importance of global sequence analysis in understanding sequence-structure relationships.