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Fig. 2 | BMC Biology

Fig. 2

From: Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation

Fig. 2

The N-terminal 25 residues of hCPEB3 adopt a hydrophobic α-helix followed by a disordered polyQ segment flanked by PQP mini-breaker motifs. The N-terminus of hCPEB3 contains an α-helix-forming and a disordered amyloidogeneic Q4RQ4 segments, which are separated by PQP mini breaker motifs. A Schematic representation as a gray cylinder of partial (20%) α-helix formation by the first ten residues of hCPEB3. The disordered conformational ensemble of residues 11–32 is represented curved lines colored purple, blue, cyan, green, orange, red, and black. B 13Cα (blue) and 13CO (black) conformational chemical shifts indicate a 20% population of helix at 25 °C. Uncertainties in the conformational chemical shifts (Δδ) are 0.02 and 0.10 ppm for 13CO and 13Cα, respectively. C {1H}-15 N NOE and D R1ρ relaxation measurements indicate that this helical conformation is less mobile than the polyQ segment at ns/ps and µs/ms timescales, respectively at 25 °C. Error bars are shown in C and D but are small as the estimated uncertainties are < 0.01 for the hNOE and < 0.1 s−1 for R1ρ. Missing values in C and D are due to overlap of 1H15N peaks or a lack of 1H15N signals in the case of proline residues (see Additional File 1. Fig. S9 for additional values from 13C-detected relaxation experiments). E Eight representative backbone conformers, colored purple, blue, teal, green, amber, orange, red, and black, of the proline rich segment, H84-Q94, featuring a PPII helix that spans residues P86-Q94. All heavy atoms are shown for the purple conformer

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