Physicochemical Analysis and Homology Modeling of Antioxidant Proteins of Foxtail Millet (Setaria Italica)
| Autor: | Shalani Gupta, Syed Mudissar Ali, Rakhi Yadav, Swati Agnihotri |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Setaria Antioxidant biology business.industry medicine.medical_treatment Protein Data Bank (RCSB PDB) Plant Science biology.organism_classification Biotechnology 03 medical and health sciences 030104 developmental biology Protein structure Biochemistry medicine Homology modeling business Peroxiredoxin Protein secondary structure Cysteine |
| Zdroj: | Vegetos- An International Journal of Plant Research. 29:33 |
| ISSN: | 2229-4473 0970-4078 |
| DOI: | 10.5958/2229-4473.2016.00008.2 |
| Popis: | Physicochemical Analysis and Homology Modeling of Antioxidant Proteins of Foxtail Millet (Setaria Italica) Foxtail Millet (Setaria italica) though falls in the category of neglected underutilized species (NUS), is considered to have very high nutritive values. It contain components that have high antioxidant activities and can reduce the blood sugar level. In this study, a bioinformatics and molecular modeling approach was adopted to explore properties and structure of foxtail millet antioxidant proteins. These antioxidant proteins include peroxiredoxins (PRDX), cysteine peroxiredoxin (CYS-PRX), ascorbic peroxidase (APX), dehydro ascorbate reductase (DHAR), and 2-Cysperoxiredoxin BASI (2CPs). Physicochemical characterization interprets properties such as isoelectric point (pI), extinction coefficient (EC), aliphatic index (AI), instability index (II) and GRAVY and provides data about these antioxidant proteins and their properties. Prediction of motifs, patterns, disulfide bridges and secondary structure were performed for functional characterization. Three dimensional structures for these proteins were not available as yet at PDB. Therefore, homology models for these antioxidant proteins were developed. The modeling of the three dimensional structure of these proteins shows that models generated by Swiss Model were more acceptable in comparison to that by Geno 3D Model. The models were validated using protein structure checking tools PROCHECK and WHAT IF. These structures will provide a good foundation for functional analysis of experimentally derived crystal structures.. |
| Databáze: | OpenAIRE |
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