Journal
ANNUAL REVIEW OF BIOPHYSICS
Volume 37, Issue -, Pages 97-116Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.37.032807.125811
Keywords
binuclear enzymes; protein aggregation; protein flexibility; proton transfer; protein-metal recognition; metal-binding residues
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This review highlights insights gained from computational studies on protein-metal recognition. We systematically dissect the various factors governing metal binding affinity and selectivity in proteins starting from (a) the intrinsic properties of the metal and neighboring metal cations (if present), to (b) the primary coordination sphere, (c) the second coordination shell, (d) the protein matrix, (e) the bulk solvent, and (f) competing non-protein ligands from the surrounding biological environment. The results herein reveal the fundamental principles and the molecular bases underlying protein-metal recognition, which serve as a guide to engineer novel metalloproteins with programmed properties.
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