Analysis of Thymine content in mRNAs and carbon content in proteins a computational approach

Abstract

Biological systems are information-rich systems. One of the major challenges today is solving the problem of genome-based diseases. There are hundreds of diseases that are reported to have their roots in the genome. These genomes underwent change during evolution, thus causing suffering to people. Though the impact is felt in all species from microorganisms to human, it is severe in mammals, particularly in human. In this context a detailed understanding of the genome, transcriptome and proteome is necessary to solve the problems of genome-based diseases. This research work focused on the role of thymine content in protein coding frames of mRNA sequences to analyze and identify the large hydrophobic residues (LHR) in protein sequences. The number and fraction of thymine in all six frames in each sequence of every species were calculated using a program written in C . This was the number and fraction of XTX in all six frames and the total number of base pairs were counted in each mRNA sequences and tabulated. Thymine is the only residue that gets changed to uracil in the base upon transcription. Protein coding frames of mRNA sequences prefers to have 27% XTX out of 100 codons such as (X= A, T, G or C). These XTXs code for large hydrophobic residues (LHRs) such as phenylalanine (F), isoleucine (I), leucine (L), methionine (M) and valine (V). Thymine in protein coding frames of mRNA sequences plays an important role in mRNA stability and activity. Therefore, the current approach tries to solve the main problems in mRNAs in the protein sequence instability. This makes the development of a tool for the genome-wide gene annotation. This research is also used to understand the role of defining thymine content in protein coding frames of mRNA sequences for protein synthesis i.e., hydrophobic interactions are the dominant force for stability in protein sequences. In human, a noticeable amount of mRNA sequences and its protein counter parts have got altered leading to malfunctioning of the proteins.