Forced Folding of a Disordered Protein Accesses an Alternative Folding Landscape. Issue 1 (24th October 2014)

• Record Type: Journal Article
• Authors: Moosa, Mahdi Muhammad; Ferreon, Allan Chris M.; Deniz, Ashok A.
• Is Part Of: Chemphyschem. Volume 16:Issue 1(2015)
• Page Start: 90
• Page End: 94
• Publication Date: 2014-10-24
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.201402661
• Languages: English
• ISSNs: 1439-4235

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Intrinsically disordered proteins (IDPs) are involved in diverse cellular functions. Many IDPs can interact with multiple binding partners, resulting in their folding into alternative ligand‐specific functional structures. For such multi‐structural IDPs, a key question is whether these multiple structures are fully encoded in the protein sequence, as is the case in many globular proteins. To answer this question, here we employed a combination of single‐molecule and ensemble techniques to compare ligand‐induced and osmolyte‐forced folding of α‐synuclein. Our results reveal context‐dependent modulation of the protein′s folding landscape, suggesting that the codes for the protein′s native folds are partially encoded in its primary sequence, and are completed only upon interaction with binding partners. Our findings suggest a critical role for cellular interactions in expanding the repertoire of folds and functions available to disordered proteins.</p> </abstract>