Who power sickle cell disease: carbon domain analysis tells all because of design in protein 3d arbitrary internal carbon domain (cod) arrangement

Several destructive diseases posing danger to the human life form (example, Ebola virus disease-EVD). Sickle cell anemia, one such disease arises from hereditary disorder. This can cause pain called sickle crises and symptoms like delayed growth and jaundice. Sickle cell disease prevents oxygen from reaching various organs of the body and causing a lot of cell death. Due to this reason, the patients get frequent infections and ultimately leading to death. The reduction in hemoglobin due to short life of the sickle cell causes anemia. The hemoglobin molecule has three components, heme group, an alpha domain and a beta domain. Patients with sickle cell disease have a mutation in the beta domain. As a result of mutation, the RBC takes a concave shape. Eaton and coworkers conclude that sickle RBC adhere to vascular endothelial cells in vitro, perhaps caused by a calciuminduced aberration of membrane topography. This adherence may be a pathogenetic factor in the microvascular occlusions characteristic of sickle cell disease.1 Verification of these adhesion possibly be the carbon role and its structural phenomena that ought to be the central point of focusing. Recently I have reported that globular proteins prefer to have 31.45% of carbon for its stability and can be used as standard for carbon distribution analysis.2–4 Allotment of carbon is responsible for disorders in proteins.5 Hydrophobic interaction is the dominant force crucial for folding.4 The content and distribution of this carbon make a protein to fold in some fashion to have a specific function. Disease proteins are expectedly differing from this carbon distribution profile.6,7 The disorders are mainly due to carbon role in different phenomena may be of evolutionary reason. Toxicity also depends on this factor of carbon role.8 CARd3D program4 exploits the availability of protein 3D structures and reveals the facts of carbon role in macromolecular folding and binding. It can play a crucial role in understanding diseases at molecular level and giving solutions in solving them. Though it is designed for globular proteins, it can be extended further for macromolecular interactions and others as well.9,10