To demonstrate the model and theory, three model proteins of hemoglobin (Hb), cytochrome C (Cyt C) and C-phycocyanin (C-PC) were chosen for the experiments.
Finally, the developed device was used for up to 8 h continuous separation of 5 mg/mL fuchsin acid and purification of three model proteins of phycocyanin, myoglobin and cytochrome C, demonstrating the applicability of FFE.
The availability of more reliable sequence search tools therefore helps to increase the success rates of the widely used approach to model proteins of unknown structures from homologous template structures [8].
To wit, mutations in the UPS can give rise to neurodegenerative disorders in both rodents and humans [ 11, 12] and sensitize organisms towards aggregation-prone model proteins of inherited neurological diseases [ 13, 14].
In order to draw general conclusions about the principles governing protein folding and unfolding, it is important to determine detailed folding information (including structural information on the transition state) for a number of model proteins of different sizes, structures and topologies.
This suggests that this method with some modifications could potentially be used for the entrapment of model proteins of somewhat smaller size (and active components more resistant to acidic conditions) that are capable of diffusion inside the matrices under proposed mild conditions.
