Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins. Aznauryan, M., Nettels, D., Holla, A., Hofmann, H., & Schuler, B. Journal of the American Chemical Society, 135(38):14040–14043, 2013. tex.ids= aznauryanSingleMoleculeSpectroscopyCold2013 ISBN: 1520-5126 (Electronic)0̊002-7863 (Linking)doi abstract bibtex 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 cold-denatured proteins are more expanded than heat-denatured 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.
@article{Aznauryan2013,
title = {Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins},
volume = {135},
issn = {00027863},
doi = {10.1021/ja407009w},
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 cold-denatured proteins are more expanded than heat-denatured 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.},
number = {38},
journal = {Journal of the American Chemical Society},
author = {Aznauryan, Mikayel and Nettels, Daniel and Holla, Andrea and Hofmann, Hagen and Schuler, Benjamin},
year = {2013},
pmid = {24010673},
note = {tex.ids= aznauryanSingleMoleculeSpectroscopyCold2013
ISBN: 1520-5126 (Electronic)0̊002-7863 (Linking)},
pages = {14040--14043},
}
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