Figure 2
From: Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2
Conformational landscapes of the phosphorylated peptides. 2D FES of WT and phosphorylated p53 peptides sampled during the REMD simulations. The X-axis represents the RMSD of each conformation of a peptide calculated from the bound form of the WT peptide from the crystal structure 1YCR16. The Y-axis represents the radius of gyration (Rg) of the peptide. Representative structures from significantly populated clusters are shown in a cartoon representation. Key binding residues Phe19, Trp23, Leu26 are shown as sticks. The percentage of structures in the corresponding clusters are given adjacent to the cartoon. The colors of the free energy surface represent the populations of the peptide conformations, and the color scheme used is shown on the right-hand side; blue and yellow correspond respectively to the highest and lowest density of conformations sampled in our REMD simulations.
