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Forced folding of a disordered protein accesses an alternative folding landscape.
- Source :
-
Chemphyschem : a European journal of chemical physics and physical chemistry [Chemphyschem] 2015 Jan 12; Vol. 16 (1), pp. 90-4. Date of Electronic Publication: 2014 Oct 24. - Publication Year :
- 2015
-
Abstract
- 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.<br /> (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Details
- Language :
- English
- ISSN :
- 1439-7641
- Volume :
- 16
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Chemphyschem : a European journal of chemical physics and physical chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 25345588
- Full Text :
- https://doi.org/10.1002/cphc.201402661