NDLI: Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins

Content Provider	PubMed Central
Author	Daniel, Nettels Sonja, Müller-späth Küster, Frank Hofmann, Hagen Haenni, Dominik Stefan, Rüegger Reymond, Luc Hoffmann, Armin Kubelka, Jan Heinz, Benjamin Gast, Klaus Best, Robert B. Schuler, Benjamin
Abstract	We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With single-molecule FRET, this question can be addressed even under near-native conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important role for additional temperature-dependent interactions within the unfolded chain. The observation of a collapse of a similar extent in the extremely hydrophilic, intrinsically disordered protein prothymosin α suggests that the hydrophobic effect is not the sole source of the underlying interactions. Circular dichroism spectroscopy and replica exchange molecular dynamics simulations in explicit water show changes in secondary structure content with increasing temperature and suggest a contribution of intramolecular hydrogen bonding to unfolded state collapse.
Related Links	http://dx.doi.org/10.1073/pnas.0900622106
Ending Page	20745
Page Count	6
Starting Page	20740
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	49
Volume Number	106
Language	English
Publisher	National Academy of Sciences
Publisher Date	2009-12-08
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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