Studies on effect of small molecules on protein folding misfolding and amyloidogenesis

Abstract

The correct folding of polypeptides to their native tertiary structure is a prerequisite for proper functioning of the proteins However despite several cellular quality control mechanisms proteins sometimes gets misfolded and trapped as aggregates The transition of proteins from their soluble globular form to insoluble fibrillar aggregates is one of the most elusive problems to modern science which has been subjected to extensive research These fibrillar aggregates sometimes exhibit high