Figure 5From: Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleftN-SH2 Tyr66 φ/ψ free-energy surfaces at 298 K and 1 atm. The open cleft conformation correlates with left-handed helical Tyr66 φ/ψ geometry and the closed cleft conformation correlates with extended Tyr66 φ/ψ geometry. Contours are every 1 kcal/mol.Back to article page