Single-molecule fluorescence studies of intrinsically disordered proteins

Ferreon, Allan Chris M., Moran, Crystal R., Gambin, Yann and Deniz, Ashok A. (2010) Single-molecule fluorescence studies of intrinsically disordered proteins. Methods in Enzymology, 472 Part A: 179-204. doi:10.1016/S0076-6879(10)72010-3


Author Ferreon, Allan Chris M.
Moran, Crystal R.
Gambin, Yann
Deniz, Ashok A.
Title Single-molecule fluorescence studies of intrinsically disordered proteins
Journal name Methods in Enzymology   Check publisher's open access policy
ISSN 1557-7988
0076-6879
1079-2376
ISBN 9780123749543
Publication date 2010
Sub-type Article (original research)
DOI 10.1016/S0076-6879(10)72010-3
Volume 472
Issue Part A
Start page 179
End page 204
Total pages 26
Editor Nils G. Walter
Place of publication Maryland Heights, MO, United States
Publisher Academic Press
Language eng
Abstract Intrinsically disordered proteins (IDPs) (also referred to as natively unfolded proteins) play critical roles in a variety of cellular processes such as transcription and translation and also are linked to several human diseases. Biophysical studies of IDPs present unusual experimental challenges due in part to their broad conformational heterogeneity and potentially complex binding-induced folding behavior. By minimizing the averaging over an ensemble (which is typical of most conventional experiments), single-molecule fluorescence (SMF) techniques have recently begun to add advanced capabilities for structural studies to the experimental arsenal of IDP investigators. Here, we briefly discuss a few common SMF methods that are particularly useful for IDP studies, including SMF resonance energy transfer and fluorescence correlation spectroscopy, along with site-specific protein-labeling methods that are essential for application of these methods to IDPs. We then present an overview of a few studies in this area, highlighting how SMF methods are being used to gain valuable information about two amyloidogenic IDPs, the Parkinson's disease-linked α-synuclein and the NM domain of the yeast prion protein Sup 35. SMF experiments provided new information about the proteins' rapidly fluctuating IDP forms, and the complex α-synuclein folding behavior upon its binding to lipid and membrane mimics. We anticipate that SMF and single-molecule methods, in general, will find broad application for structural and mechanistic studies of a wide variety of IDPs, both of their disordered conformations, and their ordered ensembles relevant for function and disease.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes Issue title: Single Molecule Tools: Fluorescence Based Approaches, Part A. Chapter 10.

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
Institute for Molecular Bioscience - Publications
 
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Created: Thu, 13 Oct 2011, 11:36:20 EST by Yann Gambin on behalf of Institute for Molecular Bioscience