Simulations of the protein folding process using topology-based models depend on the experimental structure.

Topology-based potentials (also known as Go-type models) have been widely used in the study of the protein folding problem. When a topology-based potential is applied, the structure of the native state of the protein considered has to be known in advance. This fact gives to these models a semiempirical character, and therefore the quality of the simulation results obtained for the folding transition relies, among other factors, on the accuracy of the experimental structural data employed. In this work, we use a topology-based potential to carry out folding simulations of a protein whose structure has been determined both with NMR spectroscopy and x-ray crystallography. This way, we have been able to establish to which extent the differences in the topologies of the two experimental structures, easily ignored in a standard structural analysis for this protein, affect the thermodynamic characteristics of the folding transition defined in the simulations.