As it was previously observed for RNase A variants, RNase A molecule can be divided into five segments that are formed by residues which move collectively.
The details of the residue-by-residue fluctuations induced by high pressure are very similar to those observed as a result of mutation, although the magnitude of the fluctuations in hp structures differs markedly. The problem of interpretation of the regions identified on DDM calculated for high pressure RNase structures, with ap structure as a reference,
remains a challenge.
The relatively large scale nature of these motions can result from contributions from different factors such as motions between bonded atoms, solvent effects, transitions between conformational substates of the backbone and side
chains, as well as larger cooperative fluctuations occurring in, for example, the loop regions. First explanation of observed fragmentation concerns the role of collective movements of the molecule fragments in maintaining flexibility and function of ribonuclease A.
The flexibility of the first region (residues 1–14) can be explained as a result of enzymatic cleavage of RNase A molecule.
After subtilisin cleavage action RNase A molecule is divided into S-peptide comprising residues 1–16 and S-protein that corresponds
to the rest of molecule