نتایج جستجو برای: carbon disulphide
تعداد نتایج: 283347 فیلتر نتایج به سال:
Protein disulphide isomerase (PDI) was shown to be able to accelerate the refolding of unfolded recombinant prochymosin and to enhance the overall yield of active protein. Unlike previous reports in this study PDI was found to be active at pH values as high as 11. The coincidence of the similar apparent optimum pH values of uncatalysed and PDI-catalysed reactions suggests that conditions favour...
A bacterial mixed culture able to mineralize molinate was established, through enrichment, using mineral medium with molinate as the only carbon, nitrogen and energy source. The combination of five cultivable isolates, purified from the enrichment culture, permitted the reconstitution of a degrading consortium. Both enrichment and defined cultures were able to mineralize molinate without accumu...
Disulphide Connectivity Prediction in Proteins Based on Secondary Structures and Cysteine Separation
The disulphide bonds are important in deciding the final 3D conformation of protein. Knowing disulphide connectivity will help to find out the final protein conformation, as it will limit the conformational search space. Fariselli and Casadio[1] approached problem of predicting disulphide connectivity by equating the problem to a maximum graph matching problem and assigning edge weights based o...
Hen egg white riboflavin-binding protein (RfBP) contains nine disulphide bonds. Provided these remain intact, the refolding of RfBP after incubation in 6 M guanidinium chloride is highly efficient with at least 95% of the binding activity regained within 3 min. Kinetic studies indicate that this regain consists of at least two phases. When the disulphide bonds of RfBP are reduced, reoxidation u...
We present a solution-based crystal phase engineering approach for layered transition metal disulphide nanosheets by modulating the reactivity of molecular precursors.
ERp57 is a member of the protein disulphide isomerase family of oxidoreductases, which are involved in native disulphide bond formation in the endoplasmic reticulum of mammalian cells. This enzyme has been shown to be associated with both calnexin and calreticulin and, therefore, has been proposed to be a glycoprotein-specific oxidoreductase. Here, we identify endogenous substrates for ERp57 by...
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