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4-fluorotryptophan and 5-fluorotryptophan

4-fluorotryptophan has been researched along with 5-fluorotryptophan in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19901 (25.00)18.7374
1990's3 (75.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bernstein, J; Blum, M; Bronskill, PM; Camerman, N; Grey, AA; Hofmann, T; Love, ML; Ma, LY; Wong, JT; Xu, ZJ1
Eftink, MR; Wong, CY1
Davis, SK; Eftink, MR; Maki, AH; Ozarowski, A; Wong, CY; Wu, JQ1
Budisa, N; Huber, R; Minks, C; Moroder, L1

Other Studies

4 other study(ies) available for 4-fluorotryptophan and 5-fluorotryptophan

ArticleYear
Tryptophanyl-tRNA synthetase from Bacillus subtilis. Characterization and role of hydrophobicity in substrate recognition.
    The Journal of biological chemistry, 1989, Mar-15, Volume: 264, Issue:8

    Topics: Adenosine Monophosphate; Adenosine Triphosphate; Amino Acid Sequence; Amino Acyl-tRNA Synthetases; Bacillus subtilis; Binding, Competitive; Chemical Phenomena; Chemistry, Physical; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Molecular Weight; Phosphates; RNA, Transfer, Trp; Tryptophan; Tryptophan-tRNA Ligase; X-Ray Diffraction

1989
Incorporation of tryptophan analogues into staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment: spectroscopic studies.
    Biochemistry, 1998, Jun-23, Volume: 37, Issue:25

    Topics: Amino Acid Substitution; Circular Dichroism; Fluorine; Magnetic Resonance Spectroscopy; Micrococcal Nuclease; Mutagenesis, Site-Directed; Peptide Fragments; Spectrometry, Fluorescence; Tryptophan; Valine

1998
Phosphorescence and optically detected magnetic resonance characterization of the environments of tryptophan analogues in staphylococcal nuclease, its V66W mutant, and Delta 137-149 fragment.
    Biochemistry, 1998, Jun-23, Volume: 37, Issue:25

    Topics: 5-Hydroxytryptophan; Amino Acid Substitution; Luminescent Measurements; Magnetic Resonance Spectroscopy; Micrococcal Nuclease; Mutagenesis, Site-Directed; Peptide Fragments; Tryptophan; Valine

1998
Atomic mutations at the single tryptophan residue of human recombinant annexin V: effects on structure, stability, and activity.
    Biochemistry, 1999, Aug-17, Volume: 38, Issue:33

    Topics: Annexin A5; Calcium; Circular Dichroism; Crystallization; Crystallography, X-Ray; Escherichia coli; Hot Temperature; Humans; Models, Molecular; Mutagenesis, Site-Directed; Pressure; Protein Conformation; Protein Denaturation; Recombinant Proteins; Solutions; Spectrometry, Fluorescence; Structure-Activity Relationship; Tryptophan

1999