Most of the structural properties of the proteins derive from the primary structure. The knowledge of protein structure helps in finding ways of interactions. In this report, I analyzed the physical-chemical properties of Sororin human protein to evaluate the possibility of engagement via different motifs. Also, I present data about potential disease mutations from the structural point of view.
The frequency of the mutations are shown for each amino acid. High flexibility regions are shadowed in green and the regions covering dynamical subsequences in blue
Predicted probabilities of the secondary structure of Sororin CDCA5 human protein. The regionsof comparable probabilities are highlighted in blue and the corresponding sequences are shown on the right side of the plot.
