glutamic acid and dodecyldimethylamine oxide

glutamic acid has been researched along with dodecyldimethylamine oxide in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Nakamoto, RK; Peskova, YB	1
Allison, WS; Bandyopadhyay, S; Huynh, HG; Ren, H; Valder, CR	1

Other Studies

2 other study(ies) available for glutamic acid and dodecyldimethylamine oxide

Article	Year
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. Biochemistry, 2000, Sep-26, Volume: 39, Issue:38 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. Biochemistry, 2002, Dec-03, Volume: 41, Issue:48 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

Article

Year

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.

Biochemistry, 2000, Sep-26, Volume: 39, Issue:38

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.

Biochemistry, 2002, Dec-03, Volume: 41, Issue:48

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