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. 2002 Mar;11(3):688–690. doi: 10.1110/ps.23502

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Fig. 1. — (A) The β-sheet surface of GB1 showing possible orientations for side chains Arg6, Glu53, and Arg44. In the positions shown, nitrogen–oxygen distances are 2.92 Å and 2.85 Å for residue pairs 6–53 and 44–53, respectively. Side chains were positioned with a dead-end elimination algorithm (Voigt et al. 2000) and the figure was created with MOLSCRIPT (Kraulis 1991). (B) Thermal denaturation curves for GB1 variants. From left to right (at 50% unfolded): R₆A₅₃R₄₄, R₆A₅₃A₄₄,I₆A₅₃R₄₄, I₆A₅₃A₄₄,R₆E₅₃A₄₄, I₆E₅₃A₄₄,R₆E₅₃R₄₄, and I₆E₅₃R₄₄.

Fig. 1. — (A) The β-sheet surface of GB1 showing possible orientations for side chains Arg6, Glu53, and Arg44. In the positions shown, nitrogen–oxygen distances are 2.92 Å and 2.85 Å for residue pairs 6–53 and 44–53, respectively. Side chains were positioned with a dead-end elimination algorithm (Voigt et al. 2000) and the figure was created with MOLSCRIPT (Kraulis 1991). (B) Thermal denaturation curves for GB1 variants. From left to right (at 50% unfolded): R₆A₅₃R₄₄, R₆A₅₃A₄₄,I₆A₅₃R₄₄, I₆A₅₃A₄₄,R₆E₅₃A₄₄, I₆E₅₃A₄₄,R₆E₅₃R₄₄, and I₆E₅₃R₄₄.