Physical Properties of Cd II in Thiolate Proteins

In the previous sections it has become apparent that Cd(II) thiolate complexes can be readily studied by a number of techniques. The to Cd(II) LMCT transitions observed by UV-visible and circular dichroism spectroscopy, provide a readily accessible technique for studying these systems. It has become apparent that both Cd NMR and Cd PAC spectroscopy are powerful tools with which to study these sites. Metal ion affinity, solvent exchange rates and pATa for Cd(II) binding are related to the nature of the coordination site as well as its location within the protein fold. This section will focus on the relationships that have been established between the physical properties of the Cd(II) thiolate site and the nature of these sites, using the three-stranded coiled coil family of de novo designed proteins. 

Commonly in the literature NMR chemical shifts are assigned to very 

2 Relationship between Cd(II) Coordination Geometry and pH-Dependent Binding 

The physical properties of bound Cd(II) are highly dependent on the coordination environment and geometry. As previously mentioned, monitoring the characteristic 

3 Influence of Peptide Self-Association Affinity on Cd(II) Binding 

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