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Rational Design of Protein Stability: Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin

Figure 1

Tertiary structure of human ubiquitin according to the 1.8 Å crystal structure (1UBQ.pdb).

All three proline residues (shown in red) display the Cγ-exo conformation and were simultaneously substituted with (2S,4R)-4-fluoroproline ((4R)-FPro-ub).

Figure 1

doi: https://doi.org/10.1371/journal.pone.0019425.g001