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- W2016162029 abstract "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." @default.
- W2016162029 created "2016-06-24" @default.
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- W2016162029 date "2001-02-01" @default.
- W2016162029 modified "2023-10-09" @default.
- W2016162029 title "Coiled coils: a highly versatile protein folding motif" @default.
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- W2016162029 doi "https://doi.org/10.1016/s0962-8924(00)01898-5" @default.
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