ArticleJournal, genetic engineering & biotechnology2020
In silico structural modeling and analysis of physicochemical properties of curcumin synthase (CURS1, CURS2, and CURS3) proteins of Curcuma longa.
Article in Journal, genetic engineering & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed.
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- Identification of flavonoids from natural products against hyperlipidaemia through computational approaches.PloS one · 2026Article
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- In Silico Design and Computational Elucidation of Hypothetical Resveratrol-Curcumin Hybrids as Potential Cancer Pathway Modulators.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Immunoinformatics study of CD40 ligand-targeting vaccine constructs: a novel immunotherapeutic approach.Osong public health and research perspectives · 2025Article
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- Designing of a multi-epitopes based vaccine againstFrontiers in immunology · 2024Article
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- Thermoactive metallo-keratinase fromHeliyon · 2023Article
- In Silico Analysis of the Dextransucrase Obtained FromBioinformatics and biology insights · 2023Article
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- Structure-based pharmacophore modeling, virtual screening, and molecular dynamics simulation studies for identification ofFrontiers in medicine · 2022Article
- In silico analysis of promoter region and regulatory elements of mitogenome co-expressed trn gene clusters encoding for bio-pesticide in entomopathogenic fungus, Metarhizium anisopliae: strain ME1.Journal, genetic engineering & biotechnology · 2021Article
- In silico Structural, Functional and Phylogenetic Analyses of cellulase from Ruminococcus albus.Journal, genetic engineering & biotechnology · 2021Article
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Abstract
backgroundPharmaceutically 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.
resultsThe molecular weight of CURS1 is 21093.19 Da, theoretical pI as 4.93, and an aliphatic index of 99.19. Molecular weight of CURS2 and CURS3 proteins are 20266.13 Da and 20629.52 Da, theoretical pI as 5.28 and 4.96, and an aliphatic index of 89.30 and 86.37, respectively. In the predicted secondary structure of CURS proteins, alpha helices and random coils of CURS1, CUR2, and CURS3 were 42.72, 41.38, and 44.74% and 24.87, 31.03, and 17.89, respectively. The extended strands were 16.24, 19.40, and 17.89. QMEAN Z-score is - 0.83, - 0.89, and - 1.09 for CURS1, CURS2, and CURS3, respectively.
conclusionPrediction of the 3D model of a protein by in silico analysis is a highly challenging aspect to confirm the NMR or X-ray crystallographic data. This report can contribute to the understanding of the structure, physicochemical properties, structural motifs, and protein-protein interaction of CURS1, CUR2, and CURS3.
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