Oxidative dimerization in metallothionein is a result of intermolecular disulphide bonds between cysteines in the α-domain

Keyphrases

• Cysteine 100%
• Metallothionein 100%
• Oxidative Dimerization 100%
• Intermolecular Disulfide Bond 100%
• N-terminal Domain 40%
• Disulfide Bond 40%
• Oxidative Stress 20%
• NMR Spectroscopy 20%
• Metal Ions 20%
• Tight 20%
• Metal Binding 20%
• Chemical Shift 20%
• Cysteine Disulfide 20%
• Nuclear Overhauser Effect 20%
• 1H nuclear Magnetic Resonance (1H NMR) 20%
• Cluster Structure 20%
• Molecular Mass 20%
• Conformational Exchange 20%
• Aerobic Conditions 20%
• Non-oxidative 20%
• Shift Change 20%
• Oxidation Potential 20%
• Dynamic Nature 20%
• Oxidative Processes 20%
• Metal Exchange 20%
• Cellular Oxidation 20%

Biochemistry, Genetics and Molecular Biology

• Dimerization 100%
• Disulfide Bond 100%
• Cysteine 100%
• Metallothionein 100%
• Dynamics 40%
• N-Terminus 40%
• Nuclear Magnetic Resonance Spectroscopy 20%
• Nuclear Overhauser Effect 20%
• Oxidative Stress 20%
• Molecular Weight 20%
• C-Terminus 20%
• Metal Binding 20%
• Oxidation Reduction Potential 20%
• New Species 20%