Structural properties of the truncated and wild types of Taka-amylase: A molecular dynamics simulation and docking study

- Structures of the native and truncated Taka amylase were compared.
- C-terminal domain is essential for the stability of the structure.
- The barrel region and the large cleft remained native in truncated enzymes.
- Binding affinity of maltoheptaose toward enzymes is more than those of maltotriose.