In two additional studies, Huang et al. [352,353] used PRE in their individual studies of protein binding and protein dynamics, respectively. In the Huang et al. case [352], these authors used PRE to establish a model of the binding between the G-actin protein, and thymosin β4, an actin- binding protein. Using PRE determined constraints (distances) and 1H-15N HSQC, they were able to establish a well-converging docking structure of the G-actin/thymonsin β4 complex [352]. On the other hand Huang et al. [353] did not measure protein binding, but studied the conformational changes and dynamics of select large membrane proteins utilizing 19F-NMR spectroscopy, and Ni2+ as the paramagnetic center. Through a series of extensive experiments, they showed that conformational exchange rates of membrane proteins can be determined from measurements of the metal-enhanced longitudinal relaxation (i.e., PRE) of the 19F nuclei [353], thus yielding additional information (i.e., protein conformation dynamics) that could be utilized in drug discovery projects targeting proteins (i.e., understanding how the protein changes shape based on its environment can be used to find potential binding sites for drug candidates).