Before revision:  These charts provide qualitative insights into both the folding process and the nature of the model and force field used . We demonstrate the method by conducting folding simulations on a number of small proteins which are commonly used for testing protein folding procedures: protein G, the SH3 domain of Src tyrosine kinase and chymotrypsin inhibitor 2. We compare our results for protein G to those obtained using parallel tempering with the same model. The topology of the protein molecule emerges as a major determinant of the shape of the energy landscape. The nested sampling algorithm also provides an efficient way to calculate free energies and the expectation value of thermodynamic observables at any temperature, through a simple post-processing of the output .
After revision:  These charts provide qualitative insights into both the folding process and the nature of the model and force field used .