The Role of Molecular Chaperones in Polypeptide Folding

Abstract

Purpose: The aim of the study is to examine the role of molecular chaperones in polypeptide. Methodology: This study adopted a desktop methodology. This study used secondary data from which include review of existing literature from already published studies and reports that was easily accessed through online journals and libraries. Findings: The study revealed that molecular chaperones assist in the folding of polypeptides by stabilizing intermediate folding states and preventing the aggregation of unfolded or misfolded proteins. Molecular chaperones are crucial in preventing protein misfolding and aggregation-associated diseases, particularly in the context of neurodegenerative disorders Unique Contribution to Theory, Practice and Policy: The study was anchored on The Kinetic Partitioning Model was Proposed by Susan L. Lindquist and Levinthal's Paradox and the Hierarchical Folding Model and was proposed by Cyrus Levinthal. The study recommended support funding initiatives and research grants that focus on investigating the role of molecular chaperones in protein folding and their implications in various fields, including biotechnology, medicine, and drug discovery. Promote interdisciplinary research efforts to address the challenges and opportunities associated with chaperone-mediated folding.