Figure 6
From: Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptide
Representative structures from MD simulations at different temperatures.
The figure report the structure of the centroid of the most populated clusters obtained from MD simulations at different temperatures. (a) 300 K; (b) 320 K; (c) 340 K; (d) 360 K. The side chains of the amino acids defining the hydrophobic contacts most relevant for the folding of the peptide are highlighted in light blue. The secondary structure elements were defined using the programs STRIDE74 and DSSP75.
