Evaluation of the Structural disorder of the protein FMR1 with Carbon Composition

Ever since the disorder of proteins is the main cause for many diseases. As compared with other disorders, the major reason that causes disease is of structural inability of many proteins. The potentially imminent availability of recent datasets helps one to discover the protein disorders, however in majority of cases, the stability of proteins depend on the carbon content. Addressing this distinct feature, it is possible to hit upon the carbon distribution along the sequence and can easily recognize the stable nature of protein. There are certain reported mental disorders which fall in to this category. Regardless, such kind of disorder prone protein FMR1p (Fragile X mental retardation 1 protein) is identified as the main cause for the disease Fragile X syndrome. This paper deals with the identification of defects in the FMR1 protein sequence considering the carbon contents along the sequence. This attempt is to evaluate the stability of proteins, accordingly the protein disorders in order to improvise the certain Biological functions of proteins to prevent disease. The transition of the disorder to order protein involves careful considerations and can be achieved by detecting the unstable region that lacks hydrophobicity. This work focuses the low carbon content in the FMR1 protein so as to attain the stable status in future to reduce the morbidity rate caused by Fragile X syndrome for the society.