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Christiane Jung

Max-Delbrück-Center for Molecular Medicine

Protein Dynamics Laboratory

Robert-Rössle-Strasse 10

13125 Berlin

Germany

[email]@mdc-berlin.de

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Affiliations

Max-Delbrück-Center for Molecular Medicine, Protein Dynamics Laboratory, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. 2003 - 2004
Max Delbrück Center for Molecular Medicine Berlin-Buch, Berlin, Germany. 1996 - 2002

References

High pressure fourier transform infrared (FT-IR) spectroscopic studies on inducible nitric oxide (NO) synthase active site: a comparison to cytochrome p450CAM. Jung, C., Ghosh, D.K. Cell. Mol. Biol. (Noisy-le-grand) (2004) [Pubmed]
Compressibility and uncoupling of cytochrome P450cam: high pressure FTIR and activity studies. Jung, C., Kozin, S.A., Canny, B., Chervin, J.C., Hoa, G.H. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
Cytochrome P-450-CO and substrates: lessons from ligand binding under high pressure. Jung, C. Biochim. Biophys. Acta (2002) [Pubmed]
Substrates modulate the rate-determining step for CO binding in cytochrome P450cam (CYP101). A high-pressure stopped-flow study. Jung, C., Bec, N., Lange, R. Eur. J. Biochem. (2002) [Pubmed]
FT-Infrared spectroscopic studies of the iron ligand CO stretch mode of iNOS oxygenase domain: effect of arginine and tetrahydrobiopterin. Jung, C., Stuehr, D.J., Ghosh, D.K. Biochemistry (2000) [Pubmed]
Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy. Jung, C. J. Mol. Recognit. (2000) [Pubmed]
Role of the polarity of the heme environment for the CO stretch modes in cytochrome P-450cam-CO. Jung, C., Schulze, H., Deprez, E. Biochemistry (1996) [Pubmed]