Journal of Bioinformatics, Proteomics and Imaging Analysis
Sequence to Structure Analysis of SOD1 and SOD2 from Fresh Water Turtles
- 1Bioinformatics Centre, Gauhati University, Guwahati, Assam, India
- 2School of Biological Sciences, University of Science and Technology, Meghalaya, Techno city, Baridua, India
- *RS and DKS designed the research work. Manuscript was prepared and verified by both the authors.
- #RS carried out the experiments.
Dhirendra Kumar Sharma, School of Biological Sciences, University of Science and Technology, Meghalaya, Techno city, Kiling Road, Baridua-793101, India. Tel: 91 9435147412; E-mail: firstname.lastname@example.org
Sarma, R. and Sharma, D.K., Sequence to Structure Analysis of SOD1 and SOD2 from Fresh Water Turtles. (2015) Bioinfo Proteom Img Anal 1(2): 38- 43.
© 2015 Sharma, D.K. This is an Open access article distributed under the terms of Creative Commons Attribution 4.0 International License.
KeywordsSOD1, SOD2, Structural characterization, P. sinensis, M. reevesii
Superoxide dismutase (SOD) responsible for dismutation of ROS produced in cell controls the aging and longevity of animals. An attempt has been made to report on sequence to structure analysis of the genes and proteins of SOD1 and SOD2 of freshwater turtles, Pelodiscus sinensis and Mauremys reevesii. Analysis of gene and protein sequences of these SODs retrieved from the NCBI database suggested that the there were minor variations in their molecular weight of the gene sequences, melting temperature, folding, aliphatic index and isoelectric point. Gene sequences were all AT rich with 5 restriction sites each in SOD1 of both the turtles and SOD2 of Pelodiscus sinensis while 8 restriction sites in SOD2 of Mauremys reevesii were obtained. SOD1 were dominated by β Strands, whereas, SOD2 were by the alpha helices. Homology models were generated by MODELLER 9.12 presented that all the models of SODs within acceptable range. Solvent accessible surface area (SASA) and active sites analysis of refined models of the SOD proteins were acidic and with 5 to 11 number of active sites in all the proteins and high percentage of exposed aliphatic residues. Therefore, it could well be inferred that these models have the potentiality to be used for understanding the aging process.