Understanding the influence of structural parameters is crucial to enhance the thermal stability of proteins. In this work, the stability (deltaG) of residues in different secondary structures of Ribonuclease H (RNase H) has been analyzed with 48 amino acid properties. The properties reflecting hydrophobicity show a good correlation with stability. Further, the linear distribution of surrounding hydrophobicity in alpha-helices, obtained from the three dimensional structure of thermophilic RNase H, agrees well with experimental deltaG values. Moreover, the stability parameters correlate better in alpha-helices than those did in beta-strand segments. Multiple regression analysis, incorporating combinations of three properties from among all possible combinations of the 48 properties, increased the correlation coefficient to 0.77.
Enzyme Stability Hot Temperature