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Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus

Fig 7

Per-residue secondary structure propensity and dynamics of the nsp1(13–100) designed fusion protein and the full-length globular domain of nsp1.

(A) The orange bars represent the secondary structure propensity (SSP), and the blue bars are the values predicted on the basis of the nearest amino-acid residue neighbor in the sequence using the online server: Advanced Protein Secondary Structure Prediction Server (APSSP). Positive values identify helical conformation, while negative represent extended conformation such as β-strands. The secondary structure elements extracted from the 3D solution structure of nsp1 are identified across the top. (B) Secondary structure propensity of the nsp1(13–100) designed fusion protein. The white hatched bars identify positions without data. (C) Heteronuclear 15N{1H}-NOE values of the nsp1(13–100) designed fusion protein (green bars). Positive values represent less dynamic to rigid residues, while close-to-zero and negative values identify highly dynamic residues. The standard errors are indicated. (D) Differences in the HN backbone chemical shifts (Δδ) of the nsp1(13–100) designed fusion protein compared to the full-length nsp1 protein (grey bars). The average Δδ for each secondary structure segment as well as their connecting loops are represented in red.

Fig 7

doi: https://doi.org/10.1371/journal.pone.0182132.g007