Structure Analysis and Homology Modeling of Thermostable β-galactosidase
Article
Figures
Metrics
Preview PDF
Reference
Related
Cited by
Materials
Abstract:
This study aimed to predict the primary and higher structures of thermostable β-galactosidase, providing theoretical basis for further study on its structural characteristics. Several kinds of bioinformatics softwares, including ProtParam, ProtScale, TMHMM Server v. 2.0, SignalP 4.0 Server, SOPMA, PSORT Prediction and GENO3D, were used to analyse and predict the primary and spatial structure of this enzyme. Result showed that the thermostable β-galactosidase was composed of 452 amino acids residuals. The enzyme protein had no signal peptide and transmembrane region, and located in the cytoplasm. Alpha Helix and Random coil were main structures in its secondary structure. By using homology modeling, three-dimensional structure of the enzyme was constructed.
