Alzheimer’s disease is a progressive neurodegenerative disorder characterized by deposition of amyloid plaques composed of aggregated amyloid beta plaques, and neurofibrillary tangles composed of hyperphosphorylated tau that leads to synaptic defects resulting in neuritic dystrophy and neuronal death. Diseases like Alzheimer’s are believed to result from the accumulation of mis-folded proteins. Most folded proteins have a hydrophobic core in which side chain packing stabilizes the folded state, and charged or polar side chains on the solvent-exposed surface where they interact with surrounding water molecules. In the present study, we extracted huge amounts of data from various biological databases available online. It is found that there are 74 genes that may cause Alzheimer’s disease .We evaluated the role of 74proteins that are likely to be involved in Alzheimer’s disease by employing multiple sequence alignment using ClustalW tool and constructed a Phylogenetic tree using functional protein sequences extracted from NCBI. The study also analyzed the physical properties of amino acids of functional proteins using the computational tool developed in java. These in silico study results are useful for new therapeutic interventions particularly in the field of biomarker discovery.