The structure of viral proteins can be altered by mutation to form different structures. These structural changes are caused by changes in carbon distribution. The carbon distribution statistics in viral protein samples are computed here. The statistical results are useful in identifying carbon-optimized domains and abnormal portions, such as active regions or hydrophobic parts. It clearly shows the portions of the folded protein that are exposed or buried. It is capable of locating the abnormal portion for possible mutational research. Based on this carbon distribution, mutational studies can be more effectively used to improve protein stability, activity, and, ultimately, gene therapy.
Author (s) Details
R. Devprakash
Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore–641114, Tamil Nadu, India.
K. Akila
Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore–641114, Tamil Nadu, India.
R. Senthil
Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore–641114, Tamil Nadu, India.
R. Indupriya
Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore–641114, Tamil Nadu, India.
R. Meenal
Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore–641114, Tamil Nadu, India.
E. Rajasekaran
Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore–641114, Tamil Nadu, India.
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