Prediction of potential thermostable proteins in Xylella fastidiosa

J Theor Biol. 2006 Sep 21;242(2):421-5. doi: 10.1016/j.jtbi.2006.03.009. Epub 2006 Apr 24.

Abstract

The average protein (E+K)/(Q+H) ratio in organisms has already been demonstrated to have a strong correlation with their optimal growth temperature. Employing the Thermo-Search web tool, we used this ratio as a basis to look for thermostable proteins in a mesophile, Xylella fastidiosa. Nine proteins were chosen to have their three-dimensional structures modeled by homology, using mainly proteins from mesophiles as templates. Resulting models featured a high number of hydrophobic interactions, a property that has been previously associated with thermostability. These results demonstrate the interesting possibility of using the (E+K)/(Q+H) ratio to find individual thermostable proteins in mesophilic organisms.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Chemical Phenomena
  • Chemistry, Physical
  • Hot Temperature*
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular*
  • Protein Conformation
  • Temperature
  • Xylella / chemistry*

Substances

  • Bacterial Proteins