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Figure 2 | PMC Biophysics

Figure 2

From: Probing the folding of mini-protein Beta3s by two-dimensional infrared spectroscopy; simulation study

Figure 2

The free energy surface of Beta3s and assigned conformational states. Beta3s free energy surface approximated from data in previous works by Caflisch et al. [33, 34]. Axis ΔG, Q1-2 and Q2-3 representing, free energy and fraction of native contacts in each of the strands N-terminal (strand 1), central, (strand 2) and C-terminal (Strand 3) respectively. Blue indicates low and red indicates high free energy values on a free energy scale from 0-4 kcal/mol. Conformations, a) native b) Ns c) Cs d) Ch-Curl conformations e) 6-12 Helix, are assigned to local basins in accordance free energies described in previous work [33, 34].

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