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- W2018217893 endingPage "376" @default.
- W2018217893 startingPage "363" @default.
- W2018217893 abstract "The linker regions of the central helices of calmodulin and of troponin C are observed to be α-helices in crystal and in solution. However, these linkers are predicted to be non-helical by standard algorithms. Further, there is strong evidence that when calmodulin interacts with some of its targets this linker helix bends. The linker appears to be delicately balanced between helical and non-helical conformations. A review of this subject suggests that one can anticipate more unpredicted conformations for the central helices of the score of other proteins that have four EF-hand domains." @default.
- W2018217893 created "2016-06-24" @default.
- W2018217893 creator A5035694899 @default.
- W2018217893 date "1992-06-01" @default.
- W2018217893 modified "2023-09-25" @default.
- W2018217893 title "The linker of calmodulin — to helix or not to helix" @default.
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- W2018217893 doi "https://doi.org/10.1016/0143-4160(92)90050-3" @default.
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