The Archaeal Exosome: Identification and Quantification of Site-Specific Motions That Correlate with Cap and RNA Binding
Big and unexpectedly flexible: The 173 kDa exosome core is unexpectedly dynamic in solution. The kinetic and thermodynamic properties connected with the identified exchange process were quantified. Both cap protein and RNA substrate binding significantly alter the identified motions, suggesting that...
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| Veröffentlicht in: | Angewandte Chemie International Edition 2013-08, Vol.52 (32), p.8312-8316 |
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| container_title | Angewandte Chemie International Edition |
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| creator | Audin, Maxime J. C. Dorn, Georg Fromm, Simon A. Reiss, Kerstin Schütz, Stefan Vorländer, Matthias K. Sprangers, Remco |
| description | Big and unexpectedly flexible: The 173 kDa exosome core is unexpectedly dynamic in solution. The kinetic and thermodynamic properties connected with the identified exchange process were quantified. Both cap protein and RNA substrate binding significantly alter the identified motions, suggesting that these interactions occur through conformational selection. |
| doi_str_mv | 10.1002/anie.201302811 |
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| source | MEDLINE; Wiley Journals |
| subjects | Archaea - genetics Binding Communications Correlation Dynamics Exchange exosome Exosomes - genetics Magnetic Resonance Spectroscopy molecular machines NMR spectroscopy Protein Binding protein dynamics Proteins Ribonucleic acids RNA - metabolism Thermodynamic properties |
| title | The Archaeal Exosome: Identification and Quantification of Site-Specific Motions That Correlate with Cap and RNA Binding |
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