Hochschulschrift
Pulsed EPR characterization of membrane transport protein complexes
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Maße
-
30 cm
- Umfang
-
V, 104 Bl.
- Sprache
-
Englisch
- Anmerkungen
-
Ill., graph. Darst.
Frankfurt (Main), Univ., Diss., 2012 (Nicht für den Austausch)
- Schlagwort
-
Membranproteine
Carrier-Proteine
Molekülstruktur
Strukturbiologie
Elektronenspinresonanzspektroskopie
- Urheber
- Inhaltsverzeichnis
- Rechteinformation
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Letzte Aktualisierung
-
11.03.2025, 11:38 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Objekttyp
- Hochschulschrift
Beteiligte
Ähnliche Objekte (12)
Pulsed EPR characterization of membrane transport protein complexes
Metalloproteins and protein-protein complexes investigated by CW and pulsed EPR spectroscopy
Biochemical characterization of presynaptic membrane protein complexes
EPR-Based Distance Measurements on Metal Nitroxide Model Complexes as Well as EPR Spectroscopic Characterization of [Si2]-Radicals and Titanocene Complexes
Human Telomeric Quadruplex Conformations Studied by Pulsed EPR
Pulsed EPR dipolar spectroscopy with novel paramagnetic tags
Towards single-cell pulsed EPR using VCO-based EPR-on-a-chip detectors
Light‐induced pulsed EPR dipolar spectroscopy on a paradigmatic hemeprotein
Structural characterization of membrane protein complexes by single-particle cryo-EM
Functional and structural characterization of membrane bound immunoglobulin (mIg) complexes
Conformational flexibility of multi-domain proteins determined by pulsed EPR spectroscopy
Development and application of pulsed dipolar EPR spectroscopy for physiological conditions
Pulsed EPR characterization of membrane transport protein complexes
Metalloproteins and protein-protein complexes investigated by CW and pulsed EPR spectroscopy
Biochemical characterization of presynaptic membrane protein complexes
EPR-Based Distance Measurements on Metal Nitroxide Model Complexes as Well as EPR Spectroscopic Characterization of [Si2]-Radicals and Titanocene Complexes
Human Telomeric Quadruplex Conformations Studied by Pulsed EPR
Pulsed EPR dipolar spectroscopy with novel paramagnetic tags
Towards single-cell pulsed EPR using VCO-based EPR-on-a-chip detectors
Light‐induced pulsed EPR dipolar spectroscopy on a paradigmatic hemeprotein
Structural characterization of membrane protein complexes by single-particle cryo-EM
Functional and structural characterization of membrane bound immunoglobulin (mIg) complexes
Conformational flexibility of multi-domain proteins determined by pulsed EPR spectroscopy
Development and application of pulsed dipolar EPR spectroscopy for physiological conditions
Pulsed EPR characterization of membrane transport protein complexes
Metalloproteins and protein-protein complexes investigated by CW and pulsed EPR spectroscopy
Biochemical characterization of presynaptic membrane protein complexes
EPR-Based Distance Measurements on Metal Nitroxide Model Complexes as Well as EPR Spectroscopic Characterization of [Si2]-Radicals and Titanocene Complexes
Human Telomeric Quadruplex Conformations Studied by Pulsed EPR
Pulsed EPR dipolar spectroscopy with novel paramagnetic tags
Towards single-cell pulsed EPR using VCO-based EPR-on-a-chip detectors
Light‐induced pulsed EPR dipolar spectroscopy on a paradigmatic hemeprotein
Structural characterization of membrane protein complexes by single-particle cryo-EM
Functional and structural characterization of membrane bound immunoglobulin (mIg) complexes
Conformational flexibility of multi-domain proteins determined by pulsed EPR spectroscopy