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F Bonomi

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FEBS Letters|August 15, 1979
The circular dichroism and optical absorbancy of the histidyl flavin during active-non-active transition of soluble succinate dehydrogenaseM Gutman, F Bonomi, S Pagani, et al.
European Journal of Biochemistry|January 3, 1977
Rhodanese-Mediated sulfur transfer to succinate dehydrogenaseF Bonomi, S Pagani, P Cerletti, et al.
European Journal of Biochemistry|April 1, 1996
Modifications occur at different structural levels during the heat denaturation of beta-lactoglobulinS Iametti, B De Gregori, G Vecchio, et al.
European Journal of Biochemistry|June 1, 1994
Reversible and non-denaturing replacement of iron by cadmium in Clostridium pasteurianum ferredoxinF Bonomi, M L Ganadu, G Lubinu, et al.
Biochemistry International|March 1, 1992
1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianumM L Ganadu, F Bonomi, S Pagani, et al.
The Journal of Dairy Research|April 6, 2001
Primary structure of kappa-casein isolated from mares' milkB S Iametti, G Tedeschi, E Oungre, et al.
European Journal of Biochemistry|October 28, 1997
Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the proteinH Uhlmann, S Iametti, G Vecchio, et al.
Biochimica Et Biophysica Acta|July 8, 1980
Modulation of the flavin redox potential as mode of regulation of succinate dehydrogenase activityM Gutman, F Bonomi, S Pagani, et al.
Protein Science : a Publication of the Protein Society|February 24, 2001
Thermal stability of Clostridium pasteurianum rubredoxin: deconvoluting the contributions of the metal site and the proteinF Bonomi, D Fessas, S Iametti, et al.
Biochemical and Biophysical Research Communications|July 15, 1994
Some structural features of cluster-coordinating cysteines of Clostridium pasteurianum ferredoxin are revealed by 2D TOCSY 1H NMR on the oxidized proteinD Acquotti, F Bonomi, P Brocca, et al.
Pageof 5

Showing results (21-30 of 50) with videos related to

Sort By:
Pageof 5
FEBS Letters|August 15, 1979
The circular dichroism and optical absorbancy of the histidyl flavin during active-non-active transition of soluble succinate dehydrogenaseM Gutman, F Bonomi, S Pagani, et al.
European Journal of Biochemistry|January 3, 1977
Rhodanese-Mediated sulfur transfer to succinate dehydrogenaseF Bonomi, S Pagani, P Cerletti, et al.
European Journal of Biochemistry|April 1, 1996
Modifications occur at different structural levels during the heat denaturation of beta-lactoglobulinS Iametti, B De Gregori, G Vecchio, et al.
European Journal of Biochemistry|June 1, 1994
Reversible and non-denaturing replacement of iron by cadmium in Clostridium pasteurianum ferredoxinF Bonomi, M L Ganadu, G Lubinu, et al.
Biochemistry International|March 1, 1992
1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianumM L Ganadu, F Bonomi, S Pagani, et al.
The Journal of Dairy Research|April 6, 2001
Primary structure of kappa-casein isolated from mares' milkB S Iametti, G Tedeschi, E Oungre, et al.
European Journal of Biochemistry|October 28, 1997
Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the proteinH Uhlmann, S Iametti, G Vecchio, et al.
Biochimica Et Biophysica Acta|July 8, 1980
Modulation of the flavin redox potential as mode of regulation of succinate dehydrogenase activityM Gutman, F Bonomi, S Pagani, et al.
Protein Science : a Publication of the Protein Society|February 24, 2001
Thermal stability of Clostridium pasteurianum rubredoxin: deconvoluting the contributions of the metal site and the proteinF Bonomi, D Fessas, S Iametti, et al.
Biochemical and Biophysical Research Communications|July 15, 1994
Some structural features of cluster-coordinating cysteines of Clostridium pasteurianum ferredoxin are revealed by 2D TOCSY 1H NMR on the oxidized proteinD Acquotti, F Bonomi, P Brocca, et al.
Pageof 5