Christian Altenbach
University of California, Los Angeles
75 Papers
1.3K Citations
Christian Altenbach is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Rhodopsin & Site-directed spin labeling. The author has an hindex of 43, co-authored 75 publications. Previous affiliations of Christian Altenbach include Jules Stein Eye Institute & University of California, Berkeley.
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Papers
Conformation ofspin-labeled melittin atmembranesurfaces investigated bypulse saturation recovery andcontinuous wave powersaturation electron paramagnetic resonance
Christian Altenbach,Wojciech Froncisz +1 more
- 01 Jan 1989
TL;DR: Melittin spin-labeled specifi- cally with a nitroxide atpositions 7,21, 23,ortheaminoterminus was bound to phospholipid membranes, and the exposure of thepinlabel to theaque- ous phasewas investigated bymea- surement of Heisenberg exchange with chromium oxalate inthesolution.
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Site-directed spin labeling electron paramagnetic resonance study of the ORF1 protein from a mouse L1 retrotransposon.
Kurt Januszyk,Mark R. Fleissner,Lara Atchabahian,Fa Kuen Shieh,Christian Altenbach,Sandra L. Martin,Feng Guo,Wayne L. Hubbell,Robert T. Clubb +8 more
TL;DR: A site‐directed spin labeling electron paramagnetic resonance (SDSL‐EPR) study of 27 residues within the RNA binding region of the full‐length protein suggests that these distinct surfaces are positioned adjacent to one another providing a continuous surface that may interact with nucleic acids.
The two non-visual arrestins form distinct oligomers with different functional capabilities
Qiuyan Chen,Ya Zhuo,Seunghyi Kook,Derek J. Francis,Sergey A. Vishnivetskiy,Susan M. Hanson,Xuanzhi Zhan,Evan K. Brooks,Tina M. Iverson,Christian Altenbach,Wayne L. Hubbell,Candice S. Klug,Vsevolod V. Gurevich,Vsevolod V. Gurevich,Vsevolod V. Gurevich +14 more
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A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin.
TL;DR: Ten mutants of bacteriorhodopsin, each containing a single cysteine residue regularly spaced along helix D and facing the lipid bilayer, were derivatized with a nitroxide spin label to provide a general strategy for determining the immersion depth of nitroxides in bilayers.