dodecyldimethylamine oxide has been researched along with tyrosine in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Allison, WS; Dou, C; Fortes, PA | 1 |
| Nakamoto, RK; Peskova, YB | 1 |
| Allison, WS; Bandyopadhyay, S; Huynh, HG; Ren, H; Valder, CR | 1 |
3 other study(ies) available for dodecyldimethylamine oxide and tyrosine
| Article | Year |
|---|---|
The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Azides; Bacillus; Binding Sites; Catalysis; Cattle; Cross-Linking Reagents; Detergents; Dimethylamines; Fluorescence Polarization; Hydrolysis; Kinetics; Mutagenesis, Site-Directed; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan; Tyrosine | 1998 |
Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Biological Transport; Catalysis; Cysteine; Detergents; Dimethylamines; Enzyme Activation; Escherichia coli; Glutamic Acid; Hydrolysis; Kinetics; Lysine; Methionine; Mutagenesis, Site-Directed; Peptide Fragments; Proton-Translocating ATPases; Protons; Tyrosine | 2000 |
The beta G156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Bacillus; Binding Sites; Catalysis; Catalytic Domain; Cysteine; Dimethylamines; Enzyme Stability; Glutamic Acid; Glycine; Hydrolysis; Magnesium; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Sodium Azide; Tryptophan; Tyrosine; Valine | 2002 |