Nuclear magnetic resonance proteins, lead-207 studies

One of the primary mechanisms of protein degradation is the loss of globular structure [118, 119]. This process, termed denaturation, leads to a partially or completely unfolded species which usually lacks any of the biological activity of the native protein. A variety of methods have been employed to monitor the denaturation of proteins, including fluorescence, infrared, nuclear magnetic resonance (NMR), and CD spectroscopy. As CD is very sensitive to changes in both secondary and tertiary structure, its application to the study of protein folding... 

An nuclear magnetic resonance (NMR) study of the same complex indicates that the observed hexacoordination in the crystal structure is combined with a fast exchange of the donor thioethers in solution as all carbon atoms of the side chains have equivalent signals. Even at temperatures of 183 K, the signals remain equivalent. This could lead to an extra stability, but despite the high thermodynamic stability the kinetic stability is still too low and slow exchange with serum proteins has been observed. 

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