Prediction of potential thermostable proteins in Xylella fastidiosa.
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.
Van der Linden
M G
MG
Universidade Federal da Paraíba, Departamento de Biologia Molecular, João Pessoa, PB, Brazil.
Rêgo
T G
TG
Araújo
D A M
DA
Farias
S T
ST
D001426:Bacterial Proteins / Q000737:chemistry*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D011487:Protein Conformation; D013696:Temperature; D044167:Xylella / Q000737:chemistry*
D001426:Bacterial Proteins