Protein Folding Mediated by an Intramolecular Chaperone: Energy Landscape for Unimolecular Pro-Subtilisin E Maturation
Read full paper at: http://www.scirp.org/journal/PaperInformation.aspx?PaperID=53871#.VNm4TyzQrzE Author(s) Ezhilkani Subbian , Danielle M. Williamson , Ujwal Shinde Affiliation(s) Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, USA . ABSTRACT Efficient and precise assembly of polypeptides into native functional states is critical for normal cellular processes. Understanding how a specific structure is encoded in the polypeptide sequence and what drives the structural progression to the native state is essential to deciphering the folding problem. Several prokaryotic and eukaryotic proteins require their propeptide-domains to function as dedicated intramolecular chaperones (IMCs). In this manuscript, we investigate the elementary steps in the IMC mediated maturation of Subtilisin E, a bacterial serine protease, and a prototype for the eukaryotic proprotein convertases (PCs). ...