To assess the effects of high pressure on ribonuclease A structure, we performed detailed comparison of hp (room temperature) structures with ap (low temperature) structures, therefore the temperature should be also considered as an important parameter when the protein conformational plasticity is discussed [56–58].
By analyzing the intrinsic flexibility for RNase A structures determined at different temperatures [59] and for its mutated variants [47], we reasoned that relatively larger scale of structural changes observed in hp structures arise from high pressure rather than differences in temperature during data collection or mutation.