Compounds > tryptophan

tryptophan and 4-epianhydrotetracycline

tryptophan has been researched along with 4-epianhydrotetracycline in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (25.00)18.2507
2000's3 (75.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bousquet, JA; Chabbert, M; Doglia, SM; Ettner, N; Fantucci, P; Hillen, W; Hinrichs, W; Silvi Antonini, P1
Alberti, P; Bombarda, E; Chabbert, M; Hillen, W; Kintrup, M; Kunz, M; Schneider, S; Schubert, P1
Alberti, P; Bombarda, E; Chabbert, M; Doglia, SM; Hillen, W; Kintrup, M; Lami, H; Piémont, E; Vergani, B1
Hillen, W; Kintrup, M; Kunz, M; Schneider, S1

Other Studies

4 other study(ies) available for tryptophan and 4-epianhydrotetracycline

ArticleYear
Molecular mechanics analysis of Tet repressor TRP-43 fluorescence.
    Biophysical journal, 1997, Volume: 72, Issue:4

    Topics: Dimerization; Fluorescence Polarization; Kinetics; Models, Molecular; Protein Binding; Protein Conformation; Repressor Proteins; Software; Tetracyclines; Tryptophan

1997
Trp scanning analysis of Tet repressor reveals conformational changes associated with operator and anhydrotetracycline binding.
    European journal of biochemistry, 2000, Volume: 267, Issue:3

    Topics: Bacterial Proteins; Base Sequence; DNA Primers; Energy Transfer; Escherichia coli; Fluorescence Polarization; Models, Molecular; Mutagenesis, Site-Directed; Operator Regions, Genetic; Protein Conformation; Repressor Proteins; Spectrophotometry; Tetracyclines; Tryptophan

2000
Backbone dynamics of Tet repressor alpha8intersectionalpha9 loop.
    Biochemistry, 2000, Mar-14, Volume: 39, Issue:10

    Topics: Bacterial Proteins; Energy Transfer; Fluorescence Polarization; Peptide Fragments; Protein Conformation; Protein Structure, Secondary; Repressor Proteins; Spectrometry, Fluorescence; Tetracycline; Tetracyclines; Thermodynamics; Tryptophan

2000
Conformational changes induced in the Tet repressor protein TetR(B) upon operator or anhydrotetracycline binding as revealed by time-resolved fluorescence spectroscopy on single tryptophan mutants.
    Photochemistry and photobiology, 2000, Volume: 72, Issue:1

    Topics: Bacterial Proteins; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Operator Regions, Genetic; Protein Conformation; Repressor Proteins; Spectrometry, Fluorescence; Tetracyclines; Tryptophan

2000