Kurt Warncke
Affiliations: | Physics | Emory University, Atlanta, GA |
Area:
General BiophysicsGoogle:
"Kurt Warncke"Mean distance: (not calculated yet)
Children
Sign in to add traineeJessica Hernandez-Guzman | grad student | 2010 | Emory |
Wesley D. Robertson | grad student | 2010 | Emory |
Chen Zhu | grad student | 2010 | Emory |
Adonis Bovell | grad student | 2013 | Emory |
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Publications
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Kohne M, Li W, Ionescu A, et al. (2022) Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme B-dependent ethanolamine ammonia-lyase. Methods in Enzymology. 669: 229-259 |
Li Z, Mascarenhas R, Twahir UT, et al. (2020) An interprotein Co-S coordination complex in the B12-trafficking pathway. Journal of the American Chemical Society |
Ruetz M, Campanello GC, Purchal M, et al. (2019) Itaconyl-CoA forms a stable biradical in methylmalonyl-CoA mutase and derails its activity and repair. Science (New York, N.Y.). 366: 589-593 |
Kohne M, Li W, Zhu C, et al. (2019) Deuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in B-Dependent Ethanolamine Ammonia-Lyase. Biochemistry |
Nforneh B, Warncke K. (2019) Control of Solvent Dynamics around the B-Dependent Ethanolamine Ammonia-Lyase Enzyme in Frozen Aqueous Solution by Using Dimethyl Sulfoxide Modulation of Mesodomain Volume. The Journal of Physical Chemistry. B. 123: 5395-5404 |
Ucuncuoglu N, Warncke K. (2018) Protein Configurational States Guide Radical Rearrangement Catalysis in Ethanolamine Ammonia-Lyase. Biophysical Journal. 114: 2775-2786 |
Nforneh B, Bovell AM, Warncke K. (2017) Electron spin-labelling of the EutC subunit in B12-dependent ethanolamine ammonia-lyase reveals dynamics and a two-state conformational equilibrium in the N-terminal, signal-sequence-associated domain. Free Radical Research. 1-12 |
Nforneh B, Warncke K. (2017) Mesodomain and Protein-Associated Solvent Phases with Temperature-Tunable (200-265 K) Dynamics Surround Ethanolamine Ammonia-Lyase in Globally Polycrystalline Aqueous Solution Containing Dimethyl Sulfoxide. The Journal of Physical Chemistry. B. 121: 11109-11118 |
Kohne M, Zhu C, Warncke K. (2017) Two dynamical regimes of the substrate radical rearrangement reaction in B12-dependent ethanolamine ammonia-lyase resolve contributions of native protein configurations and collective configurational fluctuations to catalysis. Biochemistry |
Wang M, Zhu C, Kohne M, et al. (2015) Resolution and Characterization of Chemical Steps in Enzyme Catalytic Sequences by Using Low-Temperature and Time-Resolved, Full-Spectrum EPR Spectroscopy in Fluid Cryosolvent and Frozen Solution Systems. Methods in Enzymology. 563: 59-94 |