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Entry ID Original Release date Data summary Entry Title Citation Title Authors
17465 2016-06-09 Kinetic Rates: 1 set
Structural Characterisation of Apoflavodoxin shows that the Location of the Stable Nucleus Differs Among Proteins with a Flavodoxin-like Topology Structural Characterisation of Apoflavodoxin shows that the Location of the Stable Nucleus Differs Among Proteins with a Flavodoxin-like Topology Download bibtex for citation iamge Carlo PM van Mierlo, Elles Steensma
4886 2000-12-04 Chemical Shifts: 1 set
Coupling Constants: 1 set
Backbone 1H and 15N and 1HB chemical shift assignments for Azotobacter vinelandii C69A apoflavodoxin Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology Download bibtex for citation iamge Carlo PM van Mierlo, Elles Steensma
4881 2000-12-05 Chemical Shifts: 1 set
Coupling Constants: 1 set
Backbone 1H, 13C, 15N and 13CB and 1HB chemical shift assignments for Azotobacter vinelandii C69A holoflavodoxin Apparent stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding Download bibtex for citation iamge Carlo PM van Mierlo, Elles Steensma, Melanie JM Nijman, P Adrie de Jager, Walter MAM van Dongen, Willy AM van den Berg, Yves JM Bollen
4800 2001-03-12 Chemical Shifts: 4 sets
Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, and of Trp109 of the isolated c domain of Paracoccus pantotrophus in the reduced state Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase Download bibtex for citation iamge Elles Steensma, Euan Gordon, Janos Hajdu, Linda M Oster, Stuart J Ferguson
4801 2001-03-12 Chemical Shifts: 4 sets
T1 Relaxation Values: 2 sets
Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, of the isolated c domain of Paracoccus pantotrophus in the oxidized state Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase Download bibtex for citation iamge Elles Steensma, Euan Gordon, Janos Hajdu, Linda M Oster, Stuart J Ferguson