Available in vitro experimental and theoretical thermodynamic data (kcal/mol) associated to the cis/trans isomerisation of peptides binding to CypA protein with the values reported for the peptide in water and bound to the protein (bold face)a.

aFor in vitro experiments ��F is about equal to ��G [10].bThermodynamic properties for a peptide having the CypA target sequence have not been determined experimentally neither in CypA nor in water solution.cFree energy differences between trans and cis minima at standard condition.dActivation free energies. The experimental ��G? values are converted from kinetic data for SUC-Ala-Phe-Pro-Phe-pNa in CypA using Transition State Theory with a prefactor of kBT/h (T = 283 K for [17], T = 273 K for [16]).eFree energy differences between trans and cis minima.fSCC-DFTB/TIP3P umbrella sampling calculation. The free energy is calculated as a function of �� (Ci-1-Oi-1-C��i-C��i) similar to �� (C��i-1-Oi-1-C��i-C��i), see Figure 2.gAmber force field umbrella sampling calculation using �� in NVE ensemble (Figure 2).hC��i-1 respective to C(i) is in the same side (clockwise) or in the opposite site (counterclockwise) of proline ring (Figure 2).