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. Author manuscript; available in PMC: 2009 Jun 23.
Published in final edited form as: J Mol Biol. 2007 Apr 20;370(1):196–206. doi: 10.1016/j.jmb.2007.04.040

Figure 1.

Figure 1

Time history of structural properties of a representative folding trajectory. From top to bottom, Cα-RMSD of the whole protein relative to the X-ray structure (PDB code 1YRF) and the two structural segments, segment A encompassing helices I and II (residues 2–20), and segment B encompassing helices II and III (residues 13–31), potential energy (kcal/mol), solvent accessible surface area (Å2), and contact order. The X-ray structure of HP35 was used as reference for RMSD calculations.