Single-Molecule Spectroscopy of Cold Denaturation and the Temperature-Induced Collapse of Unfolded Proteins.
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| 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] |
| Copyright of Journal of the American Chemical Society is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 90485322 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Single-Molecule Spectroscopy of Cold Denaturation and the Temperature-Induced Collapse of Unfolded Proteins. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Aznauryan%2C+Mikayel%22">Aznauryan, Mikayel</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Nettels%2C+Daniel%22">Nettels, Daniel</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Holla%2C+Andrea%22">Holla, Andrea</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Hofmann%2C+Hagen%22">Hofmann, Hagen</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Schuler%2C+Benjamin%22">Schuler, Benjamin</searchLink><relatesTo>1</relatesTo><i> schuler@bioc.uzh.ch</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+the+American+Chemical+Society%22">Journal of the American Chemical Society</searchLink>. 9/25/2013, Vol. 135 Issue 38, p14040-14043. 4p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Frataxin%22">Frataxin</searchLink><br /><searchLink fieldCode="DE" term="%22Fluorescence+spectroscopy%22">Fluorescence spectroscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Single+molecules+spectra%22">Single molecules spectra</searchLink><br /><searchLink fieldCode="DE" term="%22Fluorescence+resonance+energy+transfer%22">Fluorescence resonance energy transfer</searchLink><br /><searchLink fieldCode="DE" term="%22Temperature+effect%22">Temperature effect</searchLink><br /><searchLink fieldCode="DE" term="%22Heat+stability+in+proteins%22">Heat stability in proteins</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of the American Chemical Society is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1021/ja407009w Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 4 StartPage: 14040 Subjects: – SubjectFull: Denaturation of proteins Type: general – SubjectFull: Frataxin Type: general – SubjectFull: Fluorescence spectroscopy Type: general – SubjectFull: Single molecules spectra Type: general – SubjectFull: Fluorescence resonance energy transfer Type: general – SubjectFull: Temperature effect Type: general – SubjectFull: Heat stability in proteins Type: general Titles: – TitleFull: Single-Molecule Spectroscopy of Cold Denaturation and the Temperature-Induced Collapse of Unfolded Proteins. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Aznauryan, Mikayel – PersonEntity: Name: NameFull: Nettels, Daniel – PersonEntity: Name: NameFull: Holla, Andrea – PersonEntity: Name: NameFull: Hofmann, Hagen – PersonEntity: Name: NameFull: Schuler, Benjamin IsPartOfRelationships: – BibEntity: Dates: – D: 25 M: 09 Text: 9/25/2013 Type: published Y: 2013 Identifiers: – Type: issn-print Value: 00027863 Numbering: – Type: volume Value: 135 – Type: issue Value: 38 Titles: – TitleFull: Journal of the American Chemical Society Type: main |
| ResultId | 1 |
