The sequence of the metal-binding motif has a much more significant influence on Zn II) than Cu(I) affinities, and introducing the ZiaAN sequence into Atx1 and PacSN increases the Zn II) affinity by up to ∼40-fold.
Both the native pVIII and the library-selected amino acid sequences of the metal-binding peptides show a low frequency of the typical amino acids that have the highest affinity for metals [8], [9], such as histidines and cysteines [10], [11], [12].
The selectivity sequence of the studied metal was Pb2+ > Cu2+ > Zn2+ ≈ Cd2+ in single and mixed systems.
The sequence of the highest metals' concentrations in all supplements was Fe, Zn, and Mn respectively.
The stacking sequence of the three metals was copper/tin/zinc (Cu/Sn/Zn) with the Cu layer at the bottom and adjacent to the Mo layer, the Sn layer was in the middle, and the zinc layer was on the top surface.
An alignment based on the MutL pfam entries from 822 organisms was used to investigate sequence conservation of the metal-binding motif.
The sequence of the effects of metal ions on the monolayer properties and thermodynamic stability varies in the order: univalent ions < pure water < bivalent ions ≈ tervalent ions.
The poor performance of conventional short arc results from the limited ability of the power source to control every sequence of the short circuiting metal transfer mode (Lyttle and Praxair 1990; Althouse et al. 2004; Laren 2004; Goecke 2005a, b; Jeffus and Bower 2010).
