Sequence stretches in proteins that do not fold into a form are referred as disordered regions. Databases like Disport describe disordered regions in proteins and web servers like PrDOS and DisEMBL, facilitate the prediction of disordered regions. These studies are often based on residue level features. Here, we describe proteins with disordered regions using carbon content and distributions. The distribution pattern for proteins with disordered regions is different from those that do not show disordered regions.

Abstract-Hydrophobic interaction is the dominant force in proteins that arises due to carbon. The content and distribution of this carbon make a protein to fold in some form to have a specific function. Diseased proteins are expectedly differing from this carbon distribution pattern. This is taken as focus of this work by taking neurodegenerative protein, the SOD for study. The carbon distribution analysis program is able to identify the disordered region clearly. A long stretch of hydrophilic/hydrophobic regions with different combination of amino acid is considered as disordered regions. This disorder is due to unfolding or misfolding. The program developd for this purpose can further analysis the proteins for identification of mutational sites for stabilisation.

The role of hydrophobic force in biological function through the formation of several local macro-molecular structures is evident. Carbon is the element that contributes to biological function in living systems. We show that carbon distribution is related to protein activity using an example. The carbon distribution profile is foreseen to help undestand unfolded and misfolded regions of protein structures. The carbon distribution profile in a toxin protein that is found associated with the toxic shock syndrome is described in this study. The carbon profile provides insight to the association of specific residues responsible for toxicity.

Proteins function is determined by the nature of carbon along its sequence. This carbon along the protein is determined by the nucleotides in the gene. The adenine in viral genetic material and carbon distribution along its proteins are the focus of this study. The results reveal that the presence of higher adenine content in viral material add adequate number of large number of hydrophobic residues in its proteins. The natural way of adding different sequences during development and evolution is better understood based on this carbon distribution analysis. Appropriate mutation that changes in carbon content and distribution in viral proteins might improve the functionality of the protein.

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