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Christine Ebel

Showing results (1-10 of 105) with videos related to

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Methods (San Diego, Calif.)|November 30, 2010
Sedimentation velocity to characterize surfactants and solubilized membrane proteinsChristine Ebel
Acta Crystallographica. Section D, Biological Crystallography|September 28, 2002
Thermodynamic relationships between protein-solvent and protein-protein interactionsLionel Costenaro, Christine Ebel
Journal of Molecular Recognition : JMR|September 14, 2004
Crowding in extremophiles: linkage between solvation and weak protein-protein interactions, stability and dynamics, provides insight into molecular adaptationChristine Ebel, Giuseppe Zaccai
Methods in Molecular Biology (Clifton, N.J.)|December 10, 2020
Sedimentation Velocity Methods for the Characterization of Protein Heterogeneity and Protein Affinity InteractionsChristine Ebel, Catherine Birck
Biochimie|April 25, 2007
Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortuiDominique Madern, Christine Ebel
Methods in Molecular Biology (Clifton, N.J.)|February 14, 2021
Examining Membrane Proteins by Neutron ScatteringChristine Ebel, Cécile Breyton, Anne Martel
Biochemistry|October 31, 2002
Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptationLionel Costenaro, Giuseppe Zaccai, Christine Ebel
Methods in Molecular Biology (Clifton, N.J.)|July 24, 2012
Sedimentation velocity analytical ultracentrifugation for intrinsically disordered proteinsAndrés G Salvay, Guillaume Communie, Christine Ebel
Structure (London, England : 1993)|March 16, 2007
Modular structure of the full-length DNA gyrase B subunit revealed by small-angle X-ray scatteringLionel Costenaro, J Günter Grossmann, Christine Ebel, et al.
Structure (London, England : 1993)|February 9, 2005
Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunitLionel Costenaro, J Günter Grossmann, Christine Ebel, et al.
Pageof 11

Showing results (1-10 of 105) with videos related to

Sort By:
Pageof 11
Methods (San Diego, Calif.)|November 30, 2010
Sedimentation velocity to characterize surfactants and solubilized membrane proteinsChristine Ebel
Acta Crystallographica. Section D, Biological Crystallography|September 28, 2002
Thermodynamic relationships between protein-solvent and protein-protein interactionsLionel Costenaro, Christine Ebel
Journal of Molecular Recognition : JMR|September 14, 2004
Crowding in extremophiles: linkage between solvation and weak protein-protein interactions, stability and dynamics, provides insight into molecular adaptationChristine Ebel, Giuseppe Zaccai
Methods in Molecular Biology (Clifton, N.J.)|December 10, 2020
Sedimentation Velocity Methods for the Characterization of Protein Heterogeneity and Protein Affinity InteractionsChristine Ebel, Catherine Birck
Biochimie|April 25, 2007
Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortuiDominique Madern, Christine Ebel
Methods in Molecular Biology (Clifton, N.J.)|February 14, 2021
Examining Membrane Proteins by Neutron ScatteringChristine Ebel, Cécile Breyton, Anne Martel
Biochemistry|October 31, 2002
Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptationLionel Costenaro, Giuseppe Zaccai, Christine Ebel
Methods in Molecular Biology (Clifton, N.J.)|July 24, 2012
Sedimentation velocity analytical ultracentrifugation for intrinsically disordered proteinsAndrés G Salvay, Guillaume Communie, Christine Ebel
Structure (London, England : 1993)|March 16, 2007
Modular structure of the full-length DNA gyrase B subunit revealed by small-angle X-ray scatteringLionel Costenaro, J Günter Grossmann, Christine Ebel, et al.
Structure (London, England : 1993)|February 9, 2005
Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunitLionel Costenaro, J Günter Grossmann, Christine Ebel, et al.
Pageof 11