Correlation between fluorescence and structure in the orange-emitting GFP-like protein, monomeric Kusabira Orange.
Identifieur interne : 000299 ( PubMed/Curation ); précédent : 000298; suivant : 000300Correlation between fluorescence and structure in the orange-emitting GFP-like protein, monomeric Kusabira Orange.
Auteurs : A. Ausili [Italie] ; M. Staiano [Italie] ; A. Marabotti [Italie] ; G. D'Auria [Italie] ; J C G Mez-Fernández [Espagne] ; A. Torrecillas [Espagne] ; A. Ortiz [Espagne] ; S. D'Auria [Italie]Source :
- Journal of photochemistry and photobiology. B, Biology [ 1873-2682 ] ; 2014.
English descriptors
- KwdEn :
- Calorimetry, Differential Scanning, Citrus sinensis, Luminescent Proteins (chemistry), Luminescent Proteins (metabolism), Protein Denaturation, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Spectroscopy, Fourier Transform Infrared, Temperature, Thermodynamics.
- MESH :
- chemical , chemistry : Luminescent Proteins.
- chemical , metabolism : Luminescent Proteins.
- Calorimetry, Differential Scanning, Citrus sinensis, Protein Denaturation, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Spectroscopy, Fourier Transform Infrared, Temperature, Thermodynamics.
Abstract
The mKO is the monomeric version of Kusabira Orange, a GFP-like protein emitting bright orange fluorescence at 559 nm. This protein shows the characteristic β-barrel motif typical of the fluorescent protein family which it belongs to, similar spectral properties to the tetrameric form and an exceptional photo-stability to pH changes. Here, we demonstrate that mKO in solution at physiological pH exhibits a secondary structure analogue to that of the crystal. Moreover, we describe the thermal unfolding, revealing an outstanding structural stability with a denaturation temperature close to 90 °C and identifying the existence of a thermodynamic intermediate. The denaturation process of mKO results to be absolutely irreversible because of the complete lost of the native structure and the consequent aggregation, while the presence of the intermediate state is most likely due to coexistence of two different species of mKO, with protonated and deprotonated chromophore respectively, that affects the fluorescence properties and the structural stability of the protein.
DOI: 10.1016/j.jphotobiol.2014.04.028
PubMed: 24980638
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pubmed:24980638Le document en format XML
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<front><div type="abstract" xml:lang="en">The mKO is the monomeric version of Kusabira Orange, a GFP-like protein emitting bright orange fluorescence at 559 nm. This protein shows the characteristic β-barrel motif typical of the fluorescent protein family which it belongs to, similar spectral properties to the tetrameric form and an exceptional photo-stability to pH changes. Here, we demonstrate that mKO in solution at physiological pH exhibits a secondary structure analogue to that of the crystal. Moreover, we describe the thermal unfolding, revealing an outstanding structural stability with a denaturation temperature close to 90 °C and identifying the existence of a thermodynamic intermediate. The denaturation process of mKO results to be absolutely irreversible because of the complete lost of the native structure and the consequent aggregation, while the presence of the intermediate state is most likely due to coexistence of two different species of mKO, with protonated and deprotonated chromophore respectively, that affects the fluorescence properties and the structural stability of the protein.</div>
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<Abstract><AbstractText>The mKO is the monomeric version of Kusabira Orange, a GFP-like protein emitting bright orange fluorescence at 559 nm. This protein shows the characteristic β-barrel motif typical of the fluorescent protein family which it belongs to, similar spectral properties to the tetrameric form and an exceptional photo-stability to pH changes. Here, we demonstrate that mKO in solution at physiological pH exhibits a secondary structure analogue to that of the crystal. Moreover, we describe the thermal unfolding, revealing an outstanding structural stability with a denaturation temperature close to 90 °C and identifying the existence of a thermodynamic intermediate. The denaturation process of mKO results to be absolutely irreversible because of the complete lost of the native structure and the consequent aggregation, while the presence of the intermediate state is most likely due to coexistence of two different species of mKO, with protonated and deprotonated chromophore respectively, that affects the fluorescence properties and the structural stability of the protein.</AbstractText>
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