Compounds > tryptophan

tryptophan and dodecyldimethylamine oxide

tryptophan has been researched along with dodecyldimethylamine oxide in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (20.00)18.2507
2000's2 (40.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Allison, WS; Dou, C; Fortes, PA1
Choi, JW; Jung, S; Kim, HW; Lee, HW; Sohn, JH; Yeh, BI1
Allison, WS; Bandyopadhyay, S; Huynh, HG; Ren, H; Valder, CR1
Mahalakshmi, R; Maurya, SR1
Frotscher, E; Keller, S; Krainer, G; Schlierf, M1

Other Studies

5 other study(ies) available for tryptophan and dodecyldimethylamine oxide

ArticleYear
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.
    Biochemistry, 1998, Nov-24, Volume: 37, Issue:47

    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
19F NMR investigation of F(1)-ATPase of Escherichia coli using fluorotryptophan labeling.
    Journal of biochemistry, 2000, Volume: 127, Issue:6

    Topics: 4-Chloro-7-nitrobenzofurazan; Carboxypeptidases; Dimethylamines; Escherichia coli; Fluorine; Glycine; Glyphosate; Magnetic Resonance Spectroscopy; Proton-Translocating ATPases; Tryptophan

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
Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2.
    PloS one, 2014, Volume: 9, Issue:3

    Topics: Amino Acid Substitution; Cysteine; Dimethylamines; Escherichia coli; Gene Expression; Humans; Micelles; Mitochondria; Models, Molecular; Protein Folding; Protein Isoforms; Protein Stability; Protein Structure, Secondary; Recombinant Proteins; Thermodynamics; Tryptophan; Voltage-Dependent Anion Channel 2

2014
Dissecting Nanosecond Dynamics in Membrane Proteins with Dipolar Relaxation upon Tryptophan Photoexcitation.
    The journal of physical chemistry letters, 2018, May-03, Volume: 9, Issue:9

    Topics: Detergents; Dimethylamines; Fluorescence; Light; Maltose; Membrane Proteins; Micelles; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Water

2018