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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 5

Identification of hydrophobic clusters in the designed fusion proteins.

(A) Hydrophobic clusters were identified by the fluorescence intensity of bis-ANS (red bars), which was incubated with each sample, relative to the dye in the absence of protein (left axis). The accumulated hydrophobicity of GB1 domain fused to a His-tag and one of the incomplete polypeptide chains of the nsp1 protein as well as the globular domain of nsp1 are indicated as grey bars (right axis). (B) The amino acid sequence of the globular domain of nsp1 used in this study. The boundaries for each construct are indicated by numbers and hydrophobic residues (hydrophobicity > 0.8) are shown in red.

Fig 5