Bioinformatics analysis of the structural and biochemical effect of the chemical weapon mustard gas on the P53 protein and cell death
The universal and extensive usage of Sulfur Mustard gas (SM) as a disqualification chemical warfare potential in the past century has demonstrated its long-term toxic impacts. Sulfur mustard (SM), also known as mustard gas, is an alkylating compound used as a chemical weapon in World War I and by Ir...
Saved in:
| Main Author: | |
|---|---|
| Format: | Thesis |
| Language: | English |
| Published: |
2013
|
| Subjects: | |
| Online Access: | http://eprints.utm.my/id/eprint/38188/1/RitaEsmailiMFBSK2013.pdf |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | The universal and extensive usage of Sulfur Mustard gas (SM) as a disqualification chemical warfare potential in the past century has demonstrated its long-term toxic impacts. Sulfur mustard (SM), also known as mustard gas, is an alkylating compound used as a chemical weapon in World War I and by Iraqi forces against Iranians and indigenous Iraqi Kurds during the Iran–Iraq War of the 1980s. We can notice the carcinogenic effects of exposure to SM gas. The present study characterizes Bioinformatics analysis of the structural and biochemical effect of the chemical weapon mustard gas on the P53 protein and cell death. Inactivation of the p53 gene is essentially due to small mutations (missense and nonsense mutations or insertions/deletions of several nucleotides. For this study we used from Primary databases (experimental results directly into database), secondary databases (results of analysis of primary databases) and aggregate of many databases (Links to other data items, combination of data and consolidation of data).The database used includes: IARC TP53, P53web site-free, UniProt, NCBI and PDB format. Also, we used from some software in methodology such as PYMOL and CROMACS for visualizing, molecular dynamics simulation and analysis. We assay the most important of P53 region means that DNA-binding domain(DBD) from the point of view protein stability after mutation and the its effects on cell cycle arrest (cell death).The results have shown that all missense mutations selected in this case had caused remarkable flexibility and stability on DBD of the P53.Structural alterations had not been observed in DNA-binding domain, so it may be through functional changes in the certain amino acid residues and bounding linkage to DNA. |
|---|