Trends in Biotechnology
ReviewMetal-mediated protein stabilization
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2023, Enzyme and Microbial TechnologyCitation Excerpt :We have shown that Mn2+ is a rCfBGlu stabilizer and its role as a stabilizer has also been described for other β-glucosidases [24]. Frequently, two or more specific residue side chains, if positioned correctly, can form chelating sites for divalent cations that render intra-peptide crosslinking and protein stabilization [49]. The MIB2 server predicted 24 Mn2+-binding sites for the rCfBGlu structure which explain the Mn2+ stabilizing role.
Mg<sup>2+</sup> inhibits heat-induced aggregation of BSA: The mechanism and its binding site
2020, Food HydrocolloidsCitation Excerpt :The distances between Mg2+ and the two carboxylate oxygens of Asp (254) and Asp (13) fluctuated in the range of 2.010 ± 0.046 Å and 2.017 ± 0.049 Å, respectively, during the MD simulations (Fig. 4C), indicating the formation of very strong coordination bonds. Such a multivalent coordination environment will give rise to a high bond strength and allow the Mg2+ to serve as a “disulfide bridge” to crosslink the two adjacent α-helices, thereby stabilizing the secondary and tertiary structure of BSA (Arnold & Zhang, 1994). MD simulations were not only used to determine the Mg2+ binding sites, but also to investigate the structural changes caused by heating BSA in the absence or presence of Mg2+.