Do Proteins at Low Temperature Behave as Glasses? A Single-Molecule Study
We have recorded long spectral diffusion trajectories from individual LH2 pigment−protein complexes from the purple bacterium Rhodobacter sphaeroides at 1.4 K. From these data, the spectral cumulants of the absorption lines of individual, protein-embedded BChl a pigments have been evaluated. It appe...
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Veröffentlicht in: | The journal of physical chemistry. B 2007-02, Vol.111 (5), p.1135-1138 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | We have recorded long spectral diffusion trajectories from individual LH2 pigment−protein complexes from the purple bacterium Rhodobacter sphaeroides at 1.4 K. From these data, the spectral cumulants of the absorption lines of individual, protein-embedded BChl a pigments have been evaluated. It appears that the first and second cumulants cannot be described by the predictions of the well tested standard two-level system (TLS) model for spectral diffusion in glasses. The results of the present study clearly show that there is a fundamental difference between the relaxation behavior of our test protein and that of glasses. |
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ISSN: | 1520-6106 1520-5207 |
DOI: | 10.1021/jp0674569 |