DOI: 10.5176/2251-2489_BICB06
Authors: Baby Jerald, T R Gopalakriahnan Nair and Ekambaram Rajasekaran
Abstract: It is widely accepted that one of the main causes of several human diseases, pertains to the disorder of proteins. When compared to various other disorders, one of the major reasons that cause disease is the structural inability of many proteins. The vast availability of recent datasets helps one to discover the protein disorders. In this scenario, in a majority of cases, the stability of proteins depends much on the carbon content. Addressing this distinct feature, it is possible to hit upon the carbon distribution along the sequence and can 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 FMR1 (Fragile X mental retardation 1) 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 certain Biological functions of proteins to prevent diseases. The transition of the disordered to ordered 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, to reduce the morbidity rate caused by Fragile X syndrome for the society in future.
Keywords: Disorder protein, FMR1 protein, Carbon composition, Fragile X syndrome.
Updating...