RESUMO

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.

Assuntos

Proteínas de Bactérias/química , Temperatura Alta , Modelos Moleculares , Xylella/química , Fenômenos Químicos , Físico-Química , Interações Hidrofóbicas e Hidrofílicas , Conformação Proteica , Temperatura