Page last updated: 2024-08-26

acrylodan and tryptophan

acrylodan has been researched along with tryptophan in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (40.00)18.2507
2000's4 (40.00)29.6817
2010's1 (10.00)24.3611
2020's1 (10.00)2.80

Authors

AuthorsStudies
Bähler, M; Benfenati, F; Greengard, P; Masotti, L; Neyroz, P1
den Blaauwen, T; Driessen, AJ; Fekkes, P1
Cedilote, M; Clarke, RD; Peerce, BE1
Bandyopadhyay, S; Mukhopadhyay, C; Roy, S1
Slepenkov, SV; Witt, SN1
Bârzu, O; Gallay, J; Gilles, AM; Li de la Sierra, IM; Munier-Lehmann, H; Renouard, M; Sakamoto, H; Vincent, M1
Cortijo, M; González-Jiménez, J1
Krishnan, B; Kulothungan, SR; Patra, AK; Udgaonkar, JB; Varadarajan, R1
Dhanasekaran, P; Hata, M; Lund-Katz, S; Mizuguchi, C; Nickel, M; Okuhira, K; Phillips, MC; Saito, H1
Acosta, D; Das, T; Eliezer, D1

Other Studies

10 other study(ies) available for acrylodan and tryptophan

ArticleYear
Time-resolved fluorescence study of the neuron-specific phosphoprotein synapsin I. Evidence for phosphorylation-dependent conformational changes.
    The Journal of biological chemistry, 1990, Jul-25, Volume: 265, Issue:21

    Topics: 2-Naphthylamine; Animals; Cattle; Cysteine; Fluorescence Polarization; In Vitro Techniques; Maleimides; Motion; Nerve Tissue Proteins; Phosphoproteins; Phosphorylation; Protein Conformation; Spectrometry, Fluorescence; Spectrum Analysis; Sulfhydryl Reagents; Synapsins; Tryptophan

1990
Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB.
    Biochemistry, 1995, Aug-08, Volume: 34, Issue:31

    Topics: 2-Naphthylamine; Aprotinin; Bacterial Proteins; Base Sequence; Diffusion; Flow Injection Analysis; Fluorescent Dyes; Kinetics; Molecular Chaperones; Molecular Sequence Data; Protein Binding; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan

1995
Examination of the molecular mechanism of SH reagent-induced inhibition of the intestinal brush-border membrane Na+/phosphate cotransporter.
    Biochimica et biophysica acta, 1995, Oct-04, Volume: 1239, Issue:1

    Topics: 2-Naphthylamine; Affinity Labels; Animals; Carrier Proteins; Fluorescent Dyes; Fluorides; Intestinal Mucosa; Ion Transport; Microvilli; Naphthalenesulfonates; Peptide Fragments; Phosphates; Protein Conformation; Proteolipids; Rabbits; Sodium-Phosphate Cotransporter Proteins; Sulfhydryl Compounds; Sulfhydryl Reagents; Symporters; Tryptophan

1995
Dimer-dimer interfaces of the lambda-repressor are different in liganded and free states.
    Biochemistry, 1996, Apr-16, Volume: 35, Issue:15

    Topics: 2-Naphthylamine; Bacteriophage lambda; Base Sequence; Circular Dichroism; DNA-Binding Proteins; Fluorescent Dyes; Kinetics; Ligands; Molecular Sequence Data; Oligonucleotide Probes; Protein Conformation; Repressor Proteins; Tryptophan; Viral Proteins; Viral Regulatory and Accessory Proteins

1996
Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state.
    Biochemistry, 2002, Oct-08, Volume: 41, Issue:40

    Topics: 2-Naphthylamine; Adenosine Triphosphatases; Adenosine Triphosphate; Escherichia coli Proteins; Fluorescent Dyes; HSP70 Heat-Shock Proteins; Kinetics; Molecular Chaperones; Protein Structure, Tertiary; Sequence Deletion; Spectrometry, Fluorescence; Tryptophan

2002
Insight into the activation mechanism of Bordetella pertussis adenylate cyclase by calmodulin using fluorescence spectroscopy.
    European journal of biochemistry, 2004, Volume: 271, Issue:4

    Topics: 2-Naphthylamine; Acrylamide; Adenosine Triphosphate; Adenylyl Cyclases; Amino Acid Substitution; Bordetella pertussis; Calmodulin; Catalytic Domain; Entropy; Enzyme Activation; Fluorescence Polarization; Kinetics; Models, Chemical; Molecular Weight; ortho-Aminobenzoates; Protein Binding; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan

2004
Resonance energy transfer between tryptophan-214 in human serum albumin and acrylodan, prodan, and promen.
    The protein journal, 2004, Volume: 23, Issue:5

    Topics: 2-Naphthylamine; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Humans; Naphthalenes; Serum Albumin; Spectrometry, Fluorescence; Tryptophan

2004
SecB-mediated protein export need not occur via kinetic partitioning.
    Journal of molecular biology, 2009, Jan-30, Volume: 385, Issue:4

    Topics: 2-Naphthylamine; Anilino Naphthalenesulfonates; Bacterial Proteins; Carrier Proteins; Computer Simulation; Escherichia coli; Fluorescence; Kinetics; Maltose-Binding Proteins; Models, Molecular; Molecular Chaperones; Mutant Proteins; Protein Binding; Protein Folding; Protein Precursors; Protein Transport; Tryptophan

2009
Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.
    Biochimica et biophysica acta, 2014, Volume: 1841, Issue:12

    Topics: 2-Naphthylamine; Animals; Apolipoprotein E3; Apolipoprotein E4; Chickens; Fluorescence Resonance Energy Transfer; Guanidine; Humans; Kinetics; Lipids; Phosphatidylcholines; Protein Denaturation; Protein Isoforms; Protein Stability; Protein Structure, Tertiary; Pyrenes; Time Factors; Tryptophan; Unilamellar Liposomes

2014
Probing IDP Interactions with Membranes by Fluorescence Spectroscopy.
    Methods in molecular biology (Clifton, N.J.), 2020, Volume: 2141

    Topics: 2-Naphthylamine; alpha-Synuclein; Cell Membrane; Darkness; Fourier Analysis; Intrinsically Disordered Proteins; Kinetics; Light; Membrane Lipids; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Recombinant Proteins; Spectrometry, Fluorescence; tau Proteins; Tryptophan; Unilamellar Liposomes

2020