https://www.selleckchem.com/products/BIBR1532.html Correction for 'Thermo- and electro-switchable Cs⊂Fe4-Fe4 cubic cage spin-transition and electrochromism' by Jana Glatz et al., Chem. Commun., 2020, DOI 10.1039/d0cc04279j.In many products proteins have become an important component, and the long-term properties of these products are directly dependent on the stability of their proteins. To enhance this stability it has become common to add disaccharides in general, and trehalose in particular. However, the mechanisms by which disaccharides stabilize proteins and other biological materials are still not fully understood, and therefore we have here used broadband dielectric spectroscopy to investigate the stabilizing effect of the disaccharides trehalose and sucrose on myoglobin, with the aim to enhance this understanding in general and to obtain specific insights into why trehalose exhibits extraordinary stabilizing properties. The results show the existence of three or four clearly observed relaxation processes, where the three common relaxations are the local (β) water relaxation below the glass transition temperature (Tg), the structural α-relaxation of the solvent, observed above Tg, and an even slower protein relaxation duthese protein motions are slaved by the α-relaxation. Furthermore, the α-relaxation of the trehalose solution is slower than for the corresponding sucrose solution, and thereby also the protein motions become slower in the trehalose solution, which explains the more efficient stabilizing effect of trehalose on proteins above Tg.Some food and ferment manufacturing steps such as spray-drying result in the application of viscous stresses to bacteria. This study explores how a viscous flow impacts both bacterial adhesion functionality and bacterial cell organization using a combined experimental and modeling approach. As a model organism we study Lactobacillus rhamnosus GG (LGG) "wild type" (WT), known to feature strong adhesive affinities towards