Single Oligomer Spectra Probe Chromophore Nanoenvironments of Tetrameric Fluorescent Proteins.
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| Title: | Single Oligomer Spectra Probe Chromophore Nanoenvironments of Tetrameric Fluorescent Proteins. |
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| Authors: | Blum, Christian1 c.blum@utwente.nl, Meixner, Alfred J.2, Subramaniam, Vinod1 v.subramaniam@utwente.nl |
| Source: | Journal of the American Chemical Society. 7/5/2006, Vol. 128 Issue 26, p8664-8670. 7p. |
| Subjects: | Amino acid sequence, Spectrum analysis, Proteins, Biomolecules, Organic compounds |
| Abstract: | When analyzing the emission of a large number of individual chromophores embedded in a matrix, the spread of the observed parameters is a characteristic property for the particular chromophore-matrix system. To quantitatively assess the influence of the matrix on the single molecule emission parameters, it is imperative to have a system with a well-defined chromophore nanoenvironment and the possibility to alter these surroundings in a precisely controlled way. Such a system is available in the form of the visible fluorescent proteins, where the chromophore nanoenvironment is defined by the specific protein sequence. We analyze the influence of the chromophore embedding within this defined protein environment on the distribution of the emission maximum wavelength for a number of variants of the fluorescent protein DsRed, and show that this parameter is characteristic of the chromophore-protein matrix combination and largely independent of experimental conditions. We observe that the chemical changes in the vicinity of the chromophore of different variants do not account for the different distributions of emission maximum positions but that the flexibility of the chromophore surrounding has a dominant role in determining the distribution. We find, surprisingly, that the more rigid the chromophore surrounding, the broader the distribution of observed maximum positions. We hypothesize that, after a thermally induced reorientation in the chromophore surrounding, a more flexible system can easily return to its energetic minimum position by fast reorientation, while in more rigid systems the return to the energetic minimum occurs in a stepwise fashion, leading to the broader distribution observed. [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: 21525795 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Single Oligomer Spectra Probe Chromophore Nanoenvironments of Tetrameric Fluorescent Proteins. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Blum%2C+Christian%22">Blum, Christian</searchLink><relatesTo>1</relatesTo><i> c.blum@utwente.nl</i><br /><searchLink fieldCode="AR" term="%22Meixner%2C+Alfred+J%2E%22">Meixner, Alfred J.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Subramaniam%2C+Vinod%22">Subramaniam, Vinod</searchLink><relatesTo>1</relatesTo><i> v.subramaniam@utwente.nl</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>. 7/5/2006, Vol. 128 Issue 26, p8664-8670. 7p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Amino+acid+sequence%22">Amino acid sequence</searchLink><br /><searchLink fieldCode="DE" term="%22Spectrum+analysis%22">Spectrum analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Biomolecules%22">Biomolecules</searchLink><br /><searchLink fieldCode="DE" term="%22Organic+compounds%22">Organic compounds</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: When analyzing the emission of a large number of individual chromophores embedded in a matrix, the spread of the observed parameters is a characteristic property for the particular chromophore-matrix system. To quantitatively assess the influence of the matrix on the single molecule emission parameters, it is imperative to have a system with a well-defined chromophore nanoenvironment and the possibility to alter these surroundings in a precisely controlled way. Such a system is available in the form of the visible fluorescent proteins, where the chromophore nanoenvironment is defined by the specific protein sequence. We analyze the influence of the chromophore embedding within this defined protein environment on the distribution of the emission maximum wavelength for a number of variants of the fluorescent protein DsRed, and show that this parameter is characteristic of the chromophore-protein matrix combination and largely independent of experimental conditions. We observe that the chemical changes in the vicinity of the chromophore of different variants do not account for the different distributions of emission maximum positions but that the flexibility of the chromophore surrounding has a dominant role in determining the distribution. We find, surprisingly, that the more rigid the chromophore surrounding, the broader the distribution of observed maximum positions. We hypothesize that, after a thermally induced reorientation in the chromophore surrounding, a more flexible system can easily return to its energetic minimum position by fast reorientation, while in more rigid systems the return to the energetic minimum occurs in a stepwise fashion, leading to the broader distribution observed. [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/ja060726g Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 7 StartPage: 8664 Subjects: – SubjectFull: Amino acid sequence Type: general – SubjectFull: Spectrum analysis Type: general – SubjectFull: Proteins Type: general – SubjectFull: Biomolecules Type: general – SubjectFull: Organic compounds Type: general Titles: – TitleFull: Single Oligomer Spectra Probe Chromophore Nanoenvironments of Tetrameric Fluorescent Proteins. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Blum, Christian – PersonEntity: Name: NameFull: Meixner, Alfred J. – PersonEntity: Name: NameFull: Subramaniam, Vinod IsPartOfRelationships: – BibEntity: Dates: – D: 05 M: 07 Text: 7/5/2006 Type: published Y: 2006 Identifiers: – Type: issn-print Value: 00027863 Numbering: – Type: volume Value: 128 – Type: issue Value: 26 Titles: – TitleFull: Journal of the American Chemical Society Type: main |
| ResultId | 1 |
