Figure 5

The results of CHAHO algorithm for tropomyosin structure (1C1G). a) Output of hydrophobic ladder shows the presence of alanine residues at the core positions are responsible for the flexibility of the protein (alanine staggers-yellow spheres, hydrophobic residues-magenta spheres). The hydrophobic ladder has eight specific breaks. b) The method was able to identify negatively charged residue patches on the structure which could help in interacting with actin (Magenta spheres-alanine clusters, Blue spheres-actin binding sites, Red box-predicted hot spot and the residue ranges for each of the boxed region are shown). c) 1C1G structure mapped with SB, SE, DB and DE residues (SB: stabilized buried charged patches, please see text for abbreviations). Boxed region shows the destabilizing negatively charged pairs which could be responsible for the bending of mid-region in the tropomyosin structure.