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Visualization of Twitching Motility and Characterization of the Role of the PilG in Xylella fastidiosa
Published on: April 8, 2016
Prediction of potential thermostable proteins in Xylella fastidiosa
M G Van der Linden1, T G Rêgo, D A M Araújo
1Universidade Federal da Paraíba, Departamento de Biologia Molecular, João Pessoa, PB, Brazil.
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.
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