| Online-Ressource |
Verfasst von: | Gaffarogullari, Ece Cazibe [VerfasserIn]  |
| Krause, André [VerfasserIn]  |
| Balbo, Jessica [VerfasserIn]  |
| Herten, Dirk-Peter [VerfasserIn]  |
| Jäschke, Andres [VerfasserIn]  |
Titel: | Microscale thermophoresis provides insights into mechanism and thermodynamics of ribozyme catalysis |
Verf.angabe: | Ece Cazibe Gaffarogullari, André Krause, Jessica Balbo, Dirk-Peter Herten, and Andres Jäschke |
E-Jahr: | 2013 |
Jahr: | 18 Nov 2013 |
Umfang: | 7 S. |
Teil: | volume:10 |
| year:2013 |
| number:12 |
| pages:1815-1821 |
| extent:7 |
Fussnoten: | Gesehen am 04.03.2021 |
Titel Quelle: | Enthalten in: RNA biology |
Ort Quelle: | Philadelphia, Pa. : Taylor & Francis, 2004 |
Jahr Quelle: | 2013 |
Band/Heft Quelle: | 10(2013), 12, Seite 1815-1821 |
ISSN Quelle: | 1555-8584 |
Abstract: | The analysis of binding interactions between small molecules and biopolymers is important for understanding biological processes. While fluorescence correlation spectroscopy (FCS) requires fluorescence labeling on the small molecule, which often interferes with binding, in microscale thermophoresis (MST) the label can be placed on the biopolymer. Ribozymes have not been analyzed by MST so far. The Diels-Alderase ribozyme (DAse) is a true catalyst, facilitating the Diels-Alder reaction between two free small substrates, anthracene dienes, and maleimide dienophiles. Despite high efforts, the determination of the dissociation constant (KD) of maleimide dienophiles to the DAse by FCS has been unsuccessful. Here, we determined the binding interactions of the DAse to its substrates and the Diels-Alder product using MST. The results supported a positive cooperativity for substrate binding to the DAse. By varying the temperature, we furthermore studied the thermodynamics of dienophile dissociation. The entropic contribution was found to be the energetic driving force for the binding of the dienophile to the DAse. |
DOI: | doi:10.4161/rna.27101 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.4161/rna.27101 |
| DOI: https://doi.org/10.4161/rna.27101 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Diels-Alder reaction |
| fluorescence correlation spectroscopy |
| microscale thermophoresis |
| ribozyme |
| thermodynamics |
K10plus-PPN: | 1750376016 |
Verknüpfungen: | → Zeitschrift |
Microscale thermophoresis provides insights into mechanism and thermodynamics of ribozyme catalysis / Gaffarogullari, Ece Cazibe [VerfasserIn]; 18 Nov 2013 (Online-Ressource)