Applying Prim’s Algorithm to Identify Isolated Areas for Natural Disaster Prevention and Protection

Based on the principle of “pre-disaster prevention outweighs rescue during disasters”, this study targets areas threatened by natural disasters, and develops an automatic algorithm based on the Prim algorithm to serve as an automatic identification system. In the face of natural disasters that disable key facilities in the region and prevent settlements from contacting the outside world or outsiders from sending rescuers to the settlements, the proposed system helps to identify whether these regions will become isolated areas and conduct disaster mitigation and relief resource allocation before any natural disaster in order to reduce potential disaster losses. An automatic identification system, based on the threshold of channel blocking due to broken roads and bridges, determines through the decision tree model and relevant patterns whether such regions will become isolated areas by identifying areas based on the results of model analysis. The proposed system’s identification results are verified by actual case histories and comparisons;the results can be used to correctly identify isolated areas. Finally, Microsoft Visual Studio C # and Google Map are employed to apply the results and to produce an information mode for the determination and decision support of isolated areas affected by natural disasters.

Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars

D-Psicose 3-epimerase(DPEase)is demonstrated to be useful in the bioproduction of D-psicose,a rare hexose sugar,from D-fructose,found plenty in nature.Clostridium cellulolyticum H10 has recently been identified as a DPEase that can epimerize D-fructose to yield D-psicose with a much higher conversion rate when compared with the conventionally used DTEase.In this study,the crystal structure of the C.cellulolyticum DPEase was determined.The enzyme assembles into a tetramer and each subunit shows a(β/α)8 TIM barrel fold with a Mn2+metal ion in the active site.Additional crystal structures of the enzyme in complex with substrates/products(D-psicose,D-fructose,D-tagatose and D-sorbose)were also determined.From the complex structures of C.cellulolyticum DPEase with D-psicose and D-fructose,the enzyme has much more interactions with D-psicose than D-fructose by forming more hydrogen bonds between the substrate and the active site residues.Accordingly,based on these ketohexosebound complex structures,a C3-O3 proton-exchange mechanism for the conversion between D-psicose and D-fructose is proposed here.These results provide a clear idea for the deprotonation/protonation roles of E150 and E244 in catalysis.