Oxygen vacancies in oxidized and reduced vertically aligned α-MoO<sub>3</sub> nanoblades
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Materials Advances ; 3 (2022), 8. - S. 3571-3581. - Royal Society of Chemistry (RSC). - eISSN 2633-5409
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
KOPS Universität Konstanz
- (when)
-
2022
- Creator
-
Noby, Sohaila Z.
Fakharuddin, Azhar
Schupp, Stefan
Sultan, Muhammad
Krumova, Marina
Drescher, Malte
Azarkh, Mykhailo
Boldt, Klaus
Schmidt-Mende, Lukas
- URN
-
urn:nbn:de:bsz:352-2-147yntf1qqt5g3
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:26 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
- Noby, Sohaila Z.
- Fakharuddin, Azhar
- Schupp, Stefan
- Sultan, Muhammad
- Krumova, Marina
- Drescher, Malte
- Azarkh, Mykhailo
- Boldt, Klaus
- Schmidt-Mende, Lukas
- KOPS Universität Konstanz
Time of origin
- 2022
Other Objects (12)
Sportbootführerschein See für Dummies
EPR in protein science : intrinsically disordered proteins
Elektronenspinresonanz-Spektroskopie : Struktur und Dynamik intrinsisch ungeordneter Proteine
Intrazelluläre Elektronenspinresonanz-Spektroskopie
ESR-Spektroskopie zur Untersuchung der Struktur von Makromolekülen : Beitrag zur Aufklärung intrazellulärer Energieübertragung
Abstand halten : Aufklärung multivalenter Bindungsmechanismen
The effect of the zero-field splitting in light-induced pulsed dipolar electron paramagnetic resonance (EPR) spectroscopy
Dance with spins : site-directed spin labeling coupled to electron paramagnetic resonance spectroscopy directly inside cells
Background removal from rapid-scan EPR spectra of nitroxide-based spin labels by minimizing non-quadratic cost functions
Rapid Scan Electron Paramagnetic Resonance Spectroscopy Is a Suitable Tool to Study Intermolecular Interactions of Intrinsically Disordered Protein
EPR spectroscopy : applications in chemistry and biology
Conduction-Electron Drift Velocity Measurement via Electron Spin Resonance
Sportbootführerschein See für Dummies
EPR in protein science : intrinsically disordered proteins
Elektronenspinresonanz-Spektroskopie : Struktur und Dynamik intrinsisch ungeordneter Proteine
Intrazelluläre Elektronenspinresonanz-Spektroskopie
ESR-Spektroskopie zur Untersuchung der Struktur von Makromolekülen : Beitrag zur Aufklärung intrazellulärer Energieübertragung
Abstand halten : Aufklärung multivalenter Bindungsmechanismen
The effect of the zero-field splitting in light-induced pulsed dipolar electron paramagnetic resonance (EPR) spectroscopy
Dance with spins : site-directed spin labeling coupled to electron paramagnetic resonance spectroscopy directly inside cells
Background removal from rapid-scan EPR spectra of nitroxide-based spin labels by minimizing non-quadratic cost functions
Rapid Scan Electron Paramagnetic Resonance Spectroscopy Is a Suitable Tool to Study Intermolecular Interactions of Intrinsically Disordered Protein
EPR spectroscopy : applications in chemistry and biology
Conduction-Electron Drift Velocity Measurement via Electron Spin Resonance
Sportbootführerschein See für Dummies
EPR in protein science : intrinsically disordered proteins
Elektronenspinresonanz-Spektroskopie : Struktur und Dynamik intrinsisch ungeordneter Proteine
Intrazelluläre Elektronenspinresonanz-Spektroskopie
ESR-Spektroskopie zur Untersuchung der Struktur von Makromolekülen : Beitrag zur Aufklärung intrazellulärer Energieübertragung
Abstand halten : Aufklärung multivalenter Bindungsmechanismen
The effect of the zero-field splitting in light-induced pulsed dipolar electron paramagnetic resonance (EPR) spectroscopy
Dance with spins : site-directed spin labeling coupled to electron paramagnetic resonance spectroscopy directly inside cells
Background removal from rapid-scan EPR spectra of nitroxide-based spin labels by minimizing non-quadratic cost functions
Rapid Scan Electron Paramagnetic Resonance Spectroscopy Is a Suitable Tool to Study Intermolecular Interactions of Intrinsically Disordered Protein
EPR spectroscopy : applications in chemistry and biology