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• W1692912263 abstract "Fibritin is a segmented coiled-coil homotrimer of the 486-residue product of phage T4 gene wac. This protein attaches to a phage particle by the N-terminal region and forms fibrous whiskers of 530 Å, which perform a chaperone function during virus assembly. The short C-terminal region has a β-annulus-like structure. We engineered a set of fibritin deletion mutants sequentially truncated from the N-termini, and the mutants were studied by differential scanning calorimetry (DSC) and CD measurements. The analysis of␣DSC curves indicates that full-length fibritin exhibits three␣thermal-heat-absorption peaks centred at 321 K (ΔH=1390 kJ·mol trimer−1), at 336 K (ΔH=7600 kJ·mol trimer−1), and at 345 K (ΔH=515 kJ·mol trimer−1). These transitions were assigned to the N-terminal, segmented coiled-coil, and C-terminal functional domains, respectively. The coiled-coil region, containing 13 segments, melts co-operatively as a single domain with a mean enthalpy ΔHres=21 kJ·mol residue−1. The ratio of ΔHVH/ΔHcal for the coiled-coil part of the 120-, 182-, 258- and 281-residue per monomer mutants, truncated from the N-termini, and for full-length fibritin are 0.91, 0.88, 0.42, 0.39, and 0.13, respectively. This gives an indication of the decrease of the ‘all-or-none’ character of the transition with increasing protein size. The deletion of the 12-residue-long loop in the 120-residue fibritin increases the thermal stability of the coiled-coil region. According to CD data, full-length fibritin and all the mutants truncated from the N-termini refold properly after heat denaturation. In contrast, fibritin XN, which is deleted for the C-terminal domain, forms aggregates inside the cell. The XN protein can be partially refolded by dilution from urea and does not refold after heat denaturation. These results confirm that the C-terminal domain is essential for correct fibritin assembly both in vivo and in vitro and acts as a foldon." @default.
• W1692912263 created "2016-06-24" @default.
• W1692912263 creator A5033525390 @default.
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• W1692912263 date "2002-02-01" @default.
• W1692912263 modified "2023-10-06" @default.
• W1692912263 title "Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein" @default.
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• W1692912263 doi "https://doi.org/10.1046/j.1432-1033.2002.02734.x" @default.
• W1692912263 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11846809" @default.
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