Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase

Keyphrases

• Selenocysteine 100%
• Cysteine Residues 100%
• Copper Binding 100%
• Multinuclear Cluster 100%
• Copper Chaperone for Superoxide Dismutase 100%
• Spectroscopic Characterization 50%
• Expressed Protein Ligation 50%
• Redox Potential 50%
• Absorption Edge 50%
• Mutagenesis 50%
• Thiol-disulfide 50%
• Dimer Interface 50%
• Truncation 50%
• Double mutant 50%
• Oxidase Activity 50%
• Nuclearity 50%
• Tetrapeptide 50%
• Superoxide Dismutase 1 (SOD1) 50%
• XAS Studies 50%
• Triple mutant 50%
• Formation Stability 50%
• Cu-I Cluster 50%
• ATX1 50%
• Semisynthesis 50%
• Formation Potential 50%

Biochemistry, Genetics and Molecular Biology

• Selenocysteine 100%
• Superoxide Dismutase 100%
• Cysteine 100%
• Mutagenesis 50%
• Oxidoreductase 50%
• Absorption 50%
• Oxidase 50%
• Oxidation Reduction Potential 50%
• Disulfide 50%
• SOD1 50%
• Thiol 50%
• Alanine 50%
• Tetrapeptide 50%

Chemistry

• Tetrapeptide 50%