In silico structural modeling and analysis of physicochemical properties of curcumin synthase (CURS1, CURS2, and CURS3) proteins of Curcuma longa.

ABSTRACT: BACKGROUND:Pharmaceutically important curcuminoid synthesis in C. longa is controlled by CURS1, CURS2, and CURS3 genes. The present study detected the physicochemical properties and structural characteristics including the secondary and 3D structure of CURS proteins. The primary, secondary, and tertiary structure of the CURS proteins were modeled and characterized using multiple bioinformatics tools such as ExPasy ProtParam tools, self-optimized prediction method with alignment (SOPMA), PSIPRED, and SWISS-MODEL. The predicted secondary structure of curcumin synthase provided an α-helix and random coil as the major components. The reliability of the modeled structure was confirmed using PROCHECK and QMEAN programs. RESULTS:The molecular weight of CURS1 is 21093.19 Da, theoretical pI as 4.93

SUBMITTER: Santhoshkumar R 

PROVIDER: S-EPMC7332660 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature