Analysis of calculated normal modes of a set of native and partially unfolded proteins

Computations were performed for a series of conformations and various crystal structures of bovine pancreatic trypsin inhibitor (BPTI) and hen egg white lysozyme (HEWL). The goal was to investigate the influence of the multiminimum surface of the protein native state on the normal modes. Findings showed that the conformational space spanned by the 75 (BPTI) and 130 (HEWL) low-frequency normal modes, which account for about 90% of the atomic fluctuations, is relatively invariant with respect to various conformations in the native state manifold.