Molecular Dynamics of Psychrophilic Enzyme Mutants Figure 2. Hydrogen bonds and surrounding hydrophobicity (Hp) are described as histograms representing the percentage of donors+acceptors involved in H-bonds (first set, y axis on the left) or of residues with surrounding hydrophobicity in the indicated range (Hp, all other sets, y axis on the right); each set shows values computed for AHA, PPA and the mutants. doi:10.1371/journal.pone.0024214.g002 Figure 3. Rmsf in the essential subspace and surrounding hydrophobicity profiles, plotted as a function of the sequences of AHA (labels in the top row) and PPA (labels in the bottom row), and smoothed using window-averaging (window-size = 5 residues). A schematic representation of the most frequently attained secondary structure is shown in the lower plot, where a-helices of the a/b-barrel structure of domain A are labelled according to their order in the primary sequence. doi:10.1371/journal.pone.0024214.g003 PLoS ONE | www.plosone.org 3 September 2011 | Volume 6 | Issue 9 | e24214