The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The effect of temperature on ribose-5-phosphate isomerase from a mesophile, Thiobacillus thioparus, and a thermophile, Bacillus caldolyticus.

The enzyme ribose-5-phosphate isomerase [EC] was partially purified from a mesophilic organism, Thiobacillus thioparus, and from an extreme thermophile, Bacillus caldolyticus. The stability and kinetics of the two enzymes were compared with regard to temperature in the presence of a series of neutral salts and alcohols. The thermal stability of both enzymes was altered such that the salts (NH4)2SO4, NaCl, KCl, and LiCl increased stability, while LiBr, CaCl2, methanol, ethanol, and 1-propanol decreased stability. Ethylene glycol had little effect on the mesophilic enzyme, but increased the stability of the thermophilic protein. The kinetics of both enzymes were also affected by the salts and alcohols, and Arrhenius plots of two kinetic parameters, Km and Vmax, displayed discontinuities, or sharp changes in slope, at characteristic temperatures, TD. Neutral salts and alcohols altered the temperature of discontinuity in a sequence similar to that observed in studies of thermal stability. It is suggested that the slope change is due to temperature-dependent alterations in the enzymes at specific, but undefined, loci at the active site, although no evidence is offered for the absence of a larger conformation change in the entire enzyme.[1]


WikiGenes - Universities