螺旋线圈
结构母题
生物
蛋白质折叠
主题(音乐)
折叠(DSP实现)
蛋白质亚单位
蛋白质设计
低聚物
蛋白质结构
生物物理学
计算生物学
细胞生物学
生物化学
化学
物理
工程类
基因
声学
电气工程
有机化学
作者
Peter Burkhard,Jörg Stetefeld,S.V. Strelkov
标识
DOI:10.1016/s0962-8924(00)01898-5
摘要
The alpha-helical coiled coil is one of the principal subunit oligomerization motifs in proteins. Its most characteristic feature is a heptad repeat pattern of primarily apolar residues that constitute the oligomer interface. Despite its simplicity, it is a highly versatile folding motif: coiled-coil-containing proteins exhibit a broad range of different functions related to the specific 'design' of their coiled-coil domains. The architecture of a particular coiled-coil domain determines its oligomerization state, rigidity and ability to function as a molecular recognition system. Much progress has been made towards understanding the factors that determine coiled-coil formation and stability. Here we discuss this highly versatile protein folding and oligomerization motif with regard to its structural architecture and how this is related to its biological functions.
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