Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

I Bertini

Showing results (131-140 of 198) with videos related to

Pageof 20
Sort By:
European Journal of Biochemistry|March 1, 1992
1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianumI Bertini, F Briganti, C Luchinat, et al.
Biochemistry|July 22, 1997
Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome cL Banci, I Bertini, K L Bren, et al.
Biochemistry|November 1, 1988
1H NMR spectroscopic characterization of binary and ternary complexes of cobalt(II) carboxypeptidase A with inhibitorsI Bertini, C Luchinat, L Messori, et al.
Journal of Inorganic Biochemistry|June 1, 1990
Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1H NMR studies on its Cu2Co2 derivativeL Banci, I Bertini, P Caliceti, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|January 13, 2000
The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native proteinL Banci, I Bertini, R Del Conte, et al.
Biochemistry|August 5, 2000
Backbone dynamics of human Cu,Zn superoxide dismutase and of its monomeric F50E/G51E/E133Q mutant: the influence of dimerization on mobility and functionL Banci, I Bertini, F Cramaro, et al.
Biochemistry|February 9, 1988
Interaction of anions with the active site of carboxypeptidase AR Bicknell, A Schäffer, I Bertini, et al.
Biochemistry|August 26, 1998
Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?L Banci, M Benedetto, I Bertini, et al.
Biochemical and Biophysical Research Communications|December 17, 1985
Protease susceptibility of zinc- and apo-carboxypeptidase AR Bicknell, A Schaeffer, D S Auld, et al.
European Journal of Biochemistry|November 24, 1999
A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized formsM Assfalg, L Banci, I Bertini, et al.
Pageof 20

Showing results (131-140 of 198) with videos related to

Sort By:
Pageof 20
European Journal of Biochemistry|March 1, 1992
1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianumI Bertini, F Briganti, C Luchinat, et al.
Biochemistry|July 22, 1997
Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome cL Banci, I Bertini, K L Bren, et al.
Biochemistry|November 1, 1988
1H NMR spectroscopic characterization of binary and ternary complexes of cobalt(II) carboxypeptidase A with inhibitorsI Bertini, C Luchinat, L Messori, et al.
Journal of Inorganic Biochemistry|June 1, 1990
Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1H NMR studies on its Cu2Co2 derivativeL Banci, I Bertini, P Caliceti, et al.
Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|January 13, 2000
The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native proteinL Banci, I Bertini, R Del Conte, et al.
Biochemistry|August 5, 2000
Backbone dynamics of human Cu,Zn superoxide dismutase and of its monomeric F50E/G51E/E133Q mutant: the influence of dimerization on mobility and functionL Banci, I Bertini, F Cramaro, et al.
Biochemistry|February 9, 1988
Interaction of anions with the active site of carboxypeptidase AR Bicknell, A Schäffer, I Bertini, et al.
Biochemistry|August 26, 1998
Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?L Banci, M Benedetto, I Bertini, et al.
Biochemical and Biophysical Research Communications|December 17, 1985
Protease susceptibility of zinc- and apo-carboxypeptidase AR Bicknell, A Schaeffer, D S Auld, et al.
European Journal of Biochemistry|November 24, 1999
A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized formsM Assfalg, L Banci, I Bertini, et al.
Pageof 20