| Summary: | 碩士 === 國立交通大學 === 生物資訊及系統生物研究所 === 98 === Cellulose is a well-known biomass energy and plays an important role due to its abundance source to be used for producing commercially industrial products in the world. However, cellulase (Glycoside hydrolases) is referring to a class of enzymesthat hydrolyses the β-1, 4-glycosidic linkages of cellulose. And it has already been classified more than 118 families on amino acid sequence similarities that have been proposed so far, and traditionally divided into two classes denominated “endoglucanase” (EC 3.2.1.4) and “exo-glucanase” (EC 3.2.1.91). Both of them utilize the same catalytic mechanisms, and have overall similar structures. In spite of considerable structure of cellulase − function information, mechanistic studies, and catalytic site simulations seems to be well understood in recent works, there is still way to distinguish the structures between endo- and exo-glucanase being researched up to now. Therefore, in order to identify the structures of cellulase, we apply a computational method that had been developed, WCN (Weighted Contact Number) model to analyze the dynamic properties of cellulase. It means that the atom’s thermal fluctuations are in reverse proportion to the protein contact number of this atom, and a residue with lower flexibility is also more compact in proteins. Thus, through WCN model, would be helpful in binding site prediction. In summary, the fundamental purpose in this work is to realize and analyze binding site of cellulase then maybe we can recognize endo-glucanase and exo-glucanase in further. Our results provide information of cellulase protein binding site prediction. Furthermore, we can get more useful and powerful studies by using the method that we applied in the future.
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