Structural changes with temperature stability

Further insight will come only with structural studies on more of these odd catalysts. As understanding improves, protein scientists will be eager to apply this new knowledge to introduce structural changes in ordinary enzymes that would enhance temperature stability and catalytic efficiency. For the present, the microbes do it better. 

Operando methodology aims to define and characterize structure/function relationships which must be interfaced with rate and dynamics measurements of the elementary steps. Recent years have shown a marked increase in the presence of spectroscopic investigations of catalytic reactions in literature (see Catalysis Today, 113 issues 1-2). For example, operando techniques were used to determine the temperature stability range of two NOx reduction catalyst types, (NH4)[Co(H20)2]Ga(P04)3 vi. (NH4)[Mn(H20)2]Ga(P04)3. Fig. 5 shows that the catalyst with manganese changes in structural stability around 673 K. Inspection of the catalyst with cobalt shows that there is no structure modification at a temperature below 673 K. 

Spectroscopic, that is, fluorescence and circular dichroism (CD), fourier transform infared (FTIR) measurements have been widely applied to analyzing changes in enzyme structures in an attempt to explain the stabilization or denaturation phenomena associated with enzyme environments, for example, temperature, solvents, and so on. All these measurements can also be performed in ILs where fluorescence and CD spectroscopy demonstrated the conformational changes in the native structure of calcium binding proteins (CALB) which resulted in the higher s)mthetic activity and stability in ILs as compared to those obtained in classical organic solvents [18].The stabilization of enzymes by ILs may be related to the associated structural changes of proteins [19]. 

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