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- W2004141812 abstract "In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)10 by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 Å resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5° between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)10 in the designed fusion protein (GlyProPro)10foldon is higher than that of isolated (GlyProPro)10, which suggests an entropic stabilization compensating for the destabilization at the interface." @default.
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- W2004141812 date "2003-03-01" @default.
- W2004141812 modified "2023-10-10" @default.
- W2004141812 title "Collagen Stabilization at Atomic Level" @default.
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- W2004141812 doi "https://doi.org/10.1016/s0969-2126(03)00025-x" @default.
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