Pressure-induced changes in the fluorescence behavior of red fluorescent proteins
| Autor: | J. M. Weber, Ralph Jimenez, L. R. Schwall, Eric A. Pozzi |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Molecular Structure Hydrogen bond Chemistry Chromophore Photochemistry Fluorescence Fluorescence spectra Article Surfaces Coatings and Films Fluorescence intensity Luminescent Proteins Spectrometry Fluorescence Materials Chemistry Pressure Molecule Physical and Theoretical Chemistry mCherry |
| Zdroj: | The journal of physical chemistry. B. 116(34) |
| ISSN: | 1520-5207 |
| Popis: | We present an experimental study on the fluorescence behavior of the red fluorescent proteins TagRFP-S, TagRFP-T, mCherry, mOrange2, mStrawberry, and mKO as a function of pressure up to several GPa. TagRFP-S, TagRFP-T, mOrange2, and mStrawberry show an initial increase in fluorescence intensity upon application of pressure above ambient conditions. At higher pressures, the fluorescence intensity decreases dramatically for all proteins under study, probably due to denaturing of the proteins. Small blue shifts in the fluorescence spectra with increasing pressure were seen in all proteins under study, hinting at increased rigidity of the chromophore environment. In addition, mOrange2 and mStrawberry exhibit strong and abrupt changes in their fluorescence spectra at certain pressures. These changes are likely due to structural modifications of the hydrogen bonding environment of the chromophore. The strong differences in behavior between proteins with identical or very similar chromophores highlight how the chromophore environment contributes to pressure-induced behavior of the fluorescence performance. |
| Databáze: | OpenAIRE |
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