  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.
