Influence of ground-state structure and Mg2+ binding on folding kinetics of the guanine-sensing riboswitch aptamer domain
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In: Nucleic acids research 39.2011, Nr. 22, S. 9768-6778, doi:10.1093/nar/gkr664
- Classification
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Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
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Frankfurt am Main
- (who)
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Universitätsbibliothek Johann Christian Senckenberg
- (when)
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2011
- Creator
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Buck, Janina
Wacker, Anna
Warkentin, Eberhart
Wöhnert, Jens
Wirmer-Bartoschek, Julia
Schwalbe, Harald
- URN
-
urn:nbn:de:hebis:30:3-259472
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 14.08.2025, 11:01 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Buck, Janina
- Wacker, Anna
- Warkentin, Eberhart
- Wöhnert, Jens
- Wirmer-Bartoschek, Julia
- Schwalbe, Harald
- Universitätsbibliothek Johann Christian Senckenberg
Time of origin
- 2011
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Interplay of ‘induced fit’ and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch
Folding dynamics of polymorphic G-quadruplex structures
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Refolding of cold-denatured barstar induced by radio-frequency heating: a new method to study protein folding by real-time NMR spectroscopy
The cotranscriptional folding landscape for two cyclic di-nucleotide-sensing riboswitches with highly homologous aptamer domains acting either as ON- or OFF-switches
Large Temperature‐Jump and Nanosecond Hyperquenching for Time‐Resolved Structural Studies
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Dissecting the influence of Mg2+ on 3D architecture and ligand-binding of the guanine-sensing riboswitch aptamer domain
Entwicklung neuer NMR-spektroskopischer Methoden zur Bestimmung von Kopplungskonstanten an Biomakromolekülen
Bundesweite Ausbildung in NMR-Spektroskopie am BMRZ : 150 Studierende trafen sich in Frankfurt, um in NMR-Spektroskopie für ihre Master- und Doktorarbeit ausgebildet zu werden
Metal-ion binding and metal-ion induced folding of the adenine-sensing riboswitch aptamer domain
Refolding of Cold‐Denatured Barstar Induced by Radio‐Frequency Heating: A New Method to Study Protein Folding by Real‐Time NMR Spectroscopy
Interplay of ‘induced fit’ and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch
Folding dynamics of polymorphic G-quadruplex structures
Corrigendum: Folding dynamics of polymorphic G-quadruplex structures
Refolding of cold-denatured barstar induced by radio-frequency heating: a new method to study protein folding by real-time NMR spectroscopy
The cotranscriptional folding landscape for two cyclic di-nucleotide-sensing riboswitches with highly homologous aptamer domains acting either as ON- or OFF-switches
Large Temperature‐Jump and Nanosecond Hyperquenching for Time‐Resolved Structural Studies
Von Fließbandforschung und Einzelkämpfern
Dissecting the influence of Mg2+ on 3D architecture and ligand-binding of the guanine-sensing riboswitch aptamer domain
Entwicklung neuer NMR-spektroskopischer Methoden zur Bestimmung von Kopplungskonstanten an Biomakromolekülen
Bundesweite Ausbildung in NMR-Spektroskopie am BMRZ : 150 Studierende trafen sich in Frankfurt, um in NMR-Spektroskopie für ihre Master- und Doktorarbeit ausgebildet zu werden
Metal-ion binding and metal-ion induced folding of the adenine-sensing riboswitch aptamer domain
Refolding of Cold‐Denatured Barstar Induced by Radio‐Frequency Heating: A New Method to Study Protein Folding by Real‐Time NMR Spectroscopy
Interplay of ‘induced fit’ and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch
Folding dynamics of polymorphic G-quadruplex structures
Corrigendum: Folding dynamics of polymorphic G-quadruplex structures
Refolding of cold-denatured barstar induced by radio-frequency heating: a new method to study protein folding by real-time NMR spectroscopy
The cotranscriptional folding landscape for two cyclic di-nucleotide-sensing riboswitches with highly homologous aptamer domains acting either as ON- or OFF-switches
Large Temperature‐Jump and Nanosecond Hyperquenching for Time‐Resolved Structural Studies