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Oct 5, Summary. The role of metal ions in protein folding and structure is a critical topic to a range of scientists in numerous fields, particularly those. Jan 24, Protein Folding and Metal Ions: Mechanisms, Biology and Disease. Edited by Cláudio M. Gomes and Pernilla Wittung‐Stafshede. Jia‐Cherng.
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Similar Items Related Subjects: 6 Metalloproteins. Previous Figure Next Figure. A second weak class of binding sites did not permit the accurate determination of binding stoichiometry, affinity or enthalpy change of the reaction. Interestingly, zinc fingers and carbon anhydrase represent the extremes of metalloprotein design in terms of protein-folding thermodynamics due to the fact that the former are unfolded while the latter are folded in the absence of zinc. The column was charged with 1 column volume CV of 0. Given that glyoxylase is inactivated by Zn II but activated by Ni II and Co II , it is unclear whether it is a true Ni-enzyme especially since 1 zinc binds more tightly than nickel, 2 nickel proteins are virtually unknown is higher eukaryotes and 3 no known nickel homeostasis factors in humans have yet been found To further eliminate apparent nonspecific binding of proteins to IMAC, fractionation of the proteins into weakly and strongly interacting sets by electrostatic or competitive displacement with NH 4 Cl and imidazole, respectively, was conducted.
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