The correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteins - Wikidata - wikimedia - TriplyDB

The correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteins

The correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteins

http://www.wikidata.org/entity/Q36687709

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Protein design: toward functional metalloenzymes A Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed Metalloproteins Controlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.d-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.Probing a homoleptic PbS3 coordination environment in a designed peptide using 207Pb NMR spectroscopy: implications for understanding the molecular basis of lead toxicity.Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.Design of functional metalloproteins.Design of a three-helix bundle capable of binding heavy metals in a triscysteine environment.Experimental and theoretical evaluation of multisite cadmium(II) exchange in designed three-stranded coiled-coil peptides The importance of stereochemically active lone pairs for influencing Pb(II) and As(III) protein binding Designing functional metalloproteins: from structural to catalytic metal sites.Controlling self-assembly of a peptide-based material via metal-ion induced registry shift.Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution.Methods for Solving Highly Symmetric De Novo Designed Metalloproteins: Crystallographic Examination of a Novel Three-Stranded Coiled-Coil Structure Containing d-Amino Acids.Variable primary coordination environments of Cd(II) binding to three helix bundles provide a pathway for rapid metal exchange.Zinc finger proteins as templates for metal ion exchange and ligand reactivity. Chemical and biological consequences.Incorporation of second coordination sphere D-amino acids alters Cd(II) geometries in designed thiolate-rich proteins.Structural and computational insights into the versatility of cadmium binding to proteins.Lead(II) Binding in Natural and Artificial Proteins.Location dependent coordination chemistry and MRI relaxivity, in de novo designed lanthanide coiled coils.

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The correlation of 113Cd NMR and 111mCd PAC spectroscopies provides a powerful approach for the characterization of the structure of Cd(II)-substituted Zn(II) proteins

http://www.wikidata.org/entity/Q36687709

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2009 nî lūn-bûn

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2009年論文

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The correlation of 113Cd NMR a ...... I)-substituted Zn(II) proteins

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Chemistry: A European Journal

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The correlation of 113Cd NMR a ...... I)-substituted Zn(II) proteins

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Kyung-Hoon Lee

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Lars Hemmingsen

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Olga Iranzo

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Tamas Jakusch

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Vincent L Pecoraro

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3761-3772

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scholarly article

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10.1002/CHEM.200802105

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15

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15

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2009-01-01T00:00:00Z

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228049053

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19229934

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3598615

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