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Updated: Jul 4, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Bioinformatic identification of the most ancient copper protein architecture
1Shandong Provincial Research Center for Bioinformatic Engineering and Technique, Center for Advanced Study, Shandong University of Technology, Zibo 255049, PR China.
Abstract:
Since copper ions participate in many cellular processes and are implicated in pathogenesis of many diseases, copper proteins have important biological significance. Thus, it is of interest to explore their origins, especially to address the following question: which is the most ancient architecture of copper proteins? In this paper, through analyzing the architectural features of copper proteins, we find that the fold-domain relationship of these proteins follows a power law, which can be explained by preferential attachment principle and implicates that the architecture of the most ancient copper proteins belonged to Cupredoxin-like (b.6) fold. According to the chronology of protein folds, this architecture originated rather late, which can be understood in terms of the low abundance of reducing amino acids (e.g., His, Cys and/or Met) in the primordial world, because these amino acids are required by copper proteins to bind copper ions.
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