title: Factors influencing the stability of alpha-helices and beta-strands in thermophilic ribonuclease H.
abstract: 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.
authors: Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), Ibaraki, Japan.
authors: M M
authors: MM
authors: Gromiha
mesh_terms: 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
chemical_list: D012997:Solvents; D016914:Ribonuclease H