Figure 2 | Scientific Reports

Figure 2

From: Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype

Figure 2

MD simulation and generation of FfIBP mutants for disulfide bonds. (a) RMSF value for each residue during MD simulations. Flexible residues are indicated with residue numbers. (b) The overall structure of FfIBP is depicted with a cartoon representation and mutation sites for the disulfide bonds are indicated with dotted squares. (c) The putty representation of the FfIBP structure is colored by the RMSF value from the MD simulation, viewed from the same direction as in (a). Flexible residues are highlighted in different color codes. The value range is between 0.305 and 2.139 Å. (d) Close-up view of the residues mutated to cysteines for the disulfide bond. (e) The structures of mutants were determined via X-ray crystallography and the identical region shown in (d) is presented. 2Fo–Fc electron density maps contoured at 1.0 σ are displayed around the cysteines with blue mesh. MD, molecular dynamics; FfIBP, engineered ice-binding protein; RMSF, root-mean-square-fluctuation.

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