%0 Journal Article %1 desilva_selectivity_2002 %A DeSilva, Tara M %A Veglia, Gianluigi %A Porcelli, Fernando %A Prantner, Andrew M %A Opella, Stanley J %D 2002 %J Biopolymers %K Acid Amino Binding,Proteins Data,Nuclear Dichroism,Heavy,Metals,Models,Molecular,Molecular Magnetic Resonance,Peptides,Protein Sequence Sequence,Biomolecular,Biopolymers,Circular %N 4 %P 189--197 %R 10.1002/bip.10149 %T Selectivity in heavy metal- binding to peptides and proteins %V 64 %X The metal-binding affinities and three-dimensional structures of three synthetic 18-residue peptides with sequences derived from that of the highly conserved metal-binding motif MXCXXC found in many heavy metal-binding proteins were determined. A change in register of the cysteines and alanines of the sequence from the periplasmic mercury-binding protein, MerP, i.e., CAAC, CACA, and CCAA, affects the specificity of metal binding, in particular, the peptide with vicinal cysteines binds only mercury. The three-dimensional structures of the mercury-bound forms of the three peptides determined in solution by NMR spectroscopy peptides differ considerably, even though they are all linear bicoordinate complexes. The three-dimensional structure of the peptide with CAAC bound to Cd(II) demonstrates that the metal-binding loop is malleable enough to accommodate modes of coordination other than linear bicoordinate.

@article{desilva_selectivity_2002, abstract = {The metal-binding affinities and three-dimensional structures of three synthetic 18-residue peptides with sequences derived from that of the highly conserved metal-binding motif MXCXXC found in many heavy metal-binding proteins were determined. A change in register of the cysteines and alanines of the sequence from the periplasmic mercury-binding protein, MerP, i.e., CAAC, CACA, and CCAA, affects the specificity of metal binding, in particular, the peptide with vicinal cysteines binds only mercury. The three-dimensional structures of the mercury-bound forms of the three peptides determined in solution by NMR spectroscopy peptides differ considerably, even though they are all linear bicoordinate complexes. The three-dimensional structure of the peptide with CAAC bound to Cd(II) demonstrates that the metal-binding loop is malleable enough to accommodate modes of coordination other than linear bicoordinate.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {DeSilva, Tara M and Veglia, Gianluigi and Porcelli, Fernando and Prantner, Andrew M and Opella, Stanley J}, biburl = {https://www.bibsonomy.org/bibtex/22d051758461f2230f80e85426202cb2d/nmrresource}, doi = {10.1002/bip.10149}, interhash = {c49826c78b0f5611fec977665824e125}, intrahash = {2d051758461f2230f80e85426202cb2d}, issn = {0006-3525}, journal = {Biopolymers}, keywords = {Acid Amino Binding,Proteins Data,Nuclear Dichroism,Heavy,Metals,Models,Molecular,Molecular Magnetic Resonance,Peptides,Protein Sequence Sequence,Biomolecular,Biopolymers,Circular}, month = aug, number = 4, pages = {189--197}, pmid = {12115136}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Selectivity in heavy metal- binding to peptides and proteins}}, volume = 64, year = 2002 }