The possibility of predicting the overall shape of a macromolecule in solution from its diffusional properties has gained increasing importance in the structural genomic era. Here we explore and quantify the influence that unstructured and flexible regions have on the motions of a globular protein, a situation that can occur from the presence of such regions in the natural sequence or from additional tags. I27, an immunoglobulin-like module from the muscle protein titin, whose structure and properties are well characterized, was selected for our studies. The backbone dynamics and the overall tumbling of three different constructs of I27 were investigated using (15)N NMR relaxation collected at two (15)N frequencies (60.8 and 81.1 MHz) and fluorescence depolarization spectroscopy after labeling of a reactive cysteine with an extrinsic fluorophore. Our data show that the presence of disordered tags clearly exerts a frictional drag that increases with the length of the tags, thus affecting the module tumbling in solution. We discuss the use and the limitations of current approaches to hydrodynamic calculations, especially when having to take into account local flexibility.
The mill waste water holds a large amount of polyphenols, preventing the biodegradation processes because of their inhibitory action on microbial growth. Thus, its disposal represents an environmental problem for the great olive oil producing countries in the Mediterranean area. In this work, we present the preliminary results from the application of a photo-oxidative process on mill waste water to evaluate the organic matter degradation potential and the biodegradability of the treated residue. The total organic carbon is reduced up to 35% after 6 hours but the cost-effectiveness is unfavourable. In contrast, the aim of toxicity reduction is less expensive and shows good applicable chances; after 2 h, the polyphenols concentration drops by 60%.
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