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Single-Molecule Spectroscopy of Cold Denaturation and the Temperature-Induced Collapse of Unfolded Proteins.

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Bibliographic Details
Title: Single-Molecule Spectroscopy of Cold Denaturation and the Temperature-Induced Collapse of Unfolded Proteins.
Authors: Aznauryan, Mikayel1, Nettels, Daniel1, Holla, Andrea1, Hofmann, Hagen1, Schuler, Benjamin1 schuler@bioc.uzh.ch
Source: Journal of the American Chemical Society. 9/25/2013, Vol. 135 Issue 38, p14040-14043. 4p.
Subjects: Denaturation of proteins, Frataxin, Fluorescence spectroscopy, Single molecules spectra, Fluorescence resonance energy transfer, Temperature effect, Heat stability in proteins
Abstract: Recent Förster resonance energy transfer (FRET) experiments show that heat-unfolded states of proteins become more compact with increasing temperature. At the same time, NMR results indicate that colddenatured proteins are more expanded than heatdenatured proteins. To clarify the connection between these observations, we investigated the unfolded state of yeast frataxin, whose cold denaturation occurs at temperatures above 273 K, with single-molecule FRET. This method allows the unfolded state dimensions to be probed not only in the cold- and heat-denatured range but also in between, i.e., in the presence of folded protein, and can thus be used to link the two regimes directly. The results show a continuous compaction of unfolded frataxin from 274 to 320 K, with a slight re-expansion at higher temperatures. Cold- and heat-denatured states are thus essentially two sides of the same coin, and their behavior can be understood within the framework of the overall temperature dependence of the unfolded state dimensions. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
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Abstract:Recent Förster resonance energy transfer (FRET) experiments show that heat-unfolded states of proteins become more compact with increasing temperature. At the same time, NMR results indicate that colddenatured proteins are more expanded than heatdenatured proteins. To clarify the connection between these observations, we investigated the unfolded state of yeast frataxin, whose cold denaturation occurs at temperatures above 273 K, with single-molecule FRET. This method allows the unfolded state dimensions to be probed not only in the cold- and heat-denatured range but also in between, i.e., in the presence of folded protein, and can thus be used to link the two regimes directly. The results show a continuous compaction of unfolded frataxin from 274 to 320 K, with a slight re-expansion at higher temperatures. Cold- and heat-denatured states are thus essentially two sides of the same coin, and their behavior can be understood within the framework of the overall temperature dependence of the unfolded state dimensions. [ABSTRACT FROM AUTHOR]
ISSN:00027863
DOI:10.1021/ja407009w