Proteins are the most abundant macromolecules in living system. They are polymers consisting of 20 different kinds of amino acids. Each protein folds into a unique three-dimensional structure defined by its amino acid sequence. The biological function of a protein is determined by its three dimensional structure. Various factors affect protein folding,. among these factors; protein structure, post transcriptional modification, mutation and the chemical environment within the cell are the major

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... nes. Whenever there is uproar in these factors protein misfolding occurs. Protein misfoding leads to the formation of amyloid fibrils which are extracellular proteinaceous deposits found in patients suffering from any of the amyloid diseases. A broad range of human diseases arises from the failure of a specific peptide or protein to adopt, or remain in, its native functional conformation state. The pathology of such diseases underlies basically due to the formation of insoluble fiblary aggregate that resists proteolytic degradation. Such disease includes prion disease, Alzheimer"s disease, Parkinson"s disease and Huntington"s diseases. Despite the crowded cellular environment which increases chance of a newly formed protein to misfold, protein misfolding is abridged due to molecular chaperon. Molecular chaperon are proteins which aids the proper folding of a newly formed proteins by forming a non-covalent interaction. Heat sock proteins are one form of molecular chaperons.