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Journal of Thermal Analysis and Calorimetry - The water ingress phenomenon in sandwich-structured composites used in the aerospace/aeronautical sector is a current issue. This type of defect can...  相似文献   
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Journal of Thermal Analysis and Calorimetry - The aim of this work is to evaluate the potentiality of a multi-technique nondestructive approach for characterizing the state of conservation of...  相似文献   
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Four NDM-1 mutants (L218T, L221T, L269H and L221T/Y229W) were generated in order to investigate the role of leucines positioned in L10 loop. A detailed kinetic analysis stated that these amino acid substitutions modified the hydrolytic profile of NDM-1 against some β-lactams. Significant reduction of kcat values of L218T and L221T for carbapenems, cefazolin, cefoxitin and cefepime was observed. The stability of the NDM-1 and its mutants was explored by thermofluor assay in real-time PCR. The determination of TmB and TmD demonstrated that NDM-1 and L218T were the most stable enzymes. Molecular dynamic studies were performed to justify the differences observed in the kinetic behavior of the mutants. In particular, L218T fluctuated more than NDM-1 in L10, whereas L221T would seem to cause a drift between residues 75 and 125. L221T/Y229W double mutant exhibited a decrease in the flexibility with respect to L221T, explaining enzyme activity improvement towards some β-lactams. Distances between Zn1-Zn2 and Zn1-OH- or Zn2-OH- remained unaffected in all systems analysed. Significant changes were found between Zn1/Zn2 and first sphere coordination residues.  相似文献   
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Journal of Thermal Analysis and Calorimetry - This work explores the potentialities of combining a multi-layer eco-friendly panel with a phase change material coating. Although the work is based on...  相似文献   
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