Factors influencing the stability of alpha-helices and beta-strands in thermophilic ribonuclease H.
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.
Gromiha
M M
MM
Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), Ibaraki, Japan.
D004795:Enzyme Stability; D006358:Hot Temperature; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016914:Ribonuclease H / Q000737:chemistry*; D012997:Solvents; D016963:Thermus thermophilus / Q000201:enzymology
D012997:Solvents; D016914:Ribonuclease H