tryptophan has been researched along with adenylyl imidodiphosphate in 13 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (15.38) | 18.7374 |
| 1990's | 7 (53.85) | 18.2507 |
| 2000's | 4 (30.77) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Szent-Györgyi, AG | 1 |
| Güth, K | 1 |
| Senior, AE; Weber, J | 1 |
| Auzat, I; Garel, JR; Gawlita, E | 1 |
| Grell, E; Lee, RS; Senior, AE; Weber, J; Wilke-Mounts, S | 1 |
| Bowman, C; Senior, AE; Weber, J | 1 |
| de Wit, JG; den Blaauwen, T; Driessen, AJ; Fekkes, P; Kuiper, W | 1 |
| Gibbons, DL; Gorovits, BM; Hay, N; Hixson, JD; Horowitz, PM; Lund, P; Ybarra, J | 1 |
| Hammond, ST; Senior, AE; Weber, J; Wilke-Mounts, S | 1 |
| Bagshaw, CR; Málnási-Csizmadia, A; Woolley, RJ | 1 |
| Allison, WS; Dong, K; Ren, H | 1 |
| Jahn, W; Wray, J | 1 |
| Jahn, W | 1 |
13 other study(ies) available for tryptophan and adenylyl imidodiphosphate
| Article | Year |
|---|---|
Chemical and conformational events in regions of the myosin.
Topics: Actomyosin; Adenine Nucleotides; Adenosine Monophosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Binding Sites; Calcium; Cytosine Nucleotides; Ethylmaleimide; Iodides; Molecular Weight; Mollusca; Muscles; Myosin Subfragments; Myosins; Protein Conformation; Rabbits; Species Specificity; Spectrometry, Fluorescence; Troponin; Tryptophan | 1975 |
Polarization of tryptophan fluorescence measurements in muscle. A re-evaluation.
Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Fluorescence Polarization; Insecta; Muscle Contraction; Muscle Relaxation; Muscle Rigidity; Muscles; Rabbits; Tryptophan | 1980 |
Location and properties of pyrophosphate-binding sites in Escherichia coli F1-ATPase.
Topics: Adenine Nucleotides; Adenosine Monophosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Binding Sites; Binding, Competitive; Catalysis; Diphosphates; Escherichia coli; Ligands; Magnesium Compounds; Models, Chemical; Mutagenesis; Phosphates; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan | 1995 |
Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli.
Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Allosteric Regulation; Allosteric Site; Crystallography, X-Ray; Escherichia coli; Fructosephosphates; Kinetics; Ligands; Phosphoenolpyruvate; Phosphofructokinase-1; Protein Conformation; Spectrometry, Fluorescence; Time Factors; Tryptophan | 1995 |
Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Amino Acid Sequence; Base Sequence; Binding Sites; Escherichia coli; Hydrolysis; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Proton-Translocating ATPases; Recombinant Proteins; Spectrometry, Fluorescence; Tryptophan | 1993 |
Specific tryptophan substitution in catalytic sites of Escherichia coli F1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Base Sequence; Binding Sites; Catalysis; Escherichia coli; Fluorescent Dyes; Hydrolysis; Kinetics; Magnesium; Models, Biological; Molecular Sequence Data; Mutagenesis, Insertional; Oligodeoxyribonucleotides; Proton-Translocating ATPases; Spectrometry, Fluorescence; Substrate Specificity; Tryptophan | 1996 |
Domain interactions of the peripheral preprotein Translocase subunit SecA.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenylyl Imidodiphosphate; Amino Acid Sequence; Bacterial Proteins; Calorimetry, Differential Scanning; Escherichia coli; Escherichia coli Proteins; Membrane Transport Proteins; Models, Chemical; Mutagenesis, Site-Directed; Peptide Fragments; Recombinant Proteins; Restriction Mapping; Scattering, Radiation; SEC Translocation Channels; SecA Proteins; Sequence Deletion; Spectrometry, Fluorescence; Thermodynamics; Trypsin; Tryptophan | 1996 |
Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr --> Trp replacements reveal ligand-induced conformational changes.
Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Chaperonin 60; Magnesium; Mutagenesis, Site-Directed; Potassium; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; Tyrosine | 1996 |
Tryptophan substitutions surrounding the nucleotide in catalytic sites of F1-ATPase.
Topics: Adenine Nucleotides; Adenylyl Imidodiphosphate; Amino Acid Substitution; Binding Sites; Catalysis; Escherichia coli; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Protein Engineering; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan | 1998 |
Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Aluminum Compounds; Animals; Binding Sites; Crystallography, X-Ray; Dictyostelium; Fluorides; Hydrolysis; Kinetics; Molecular Motor Proteins; Mutagenesis, Site-Directed; Myosins; Protein Conformation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan | 2000 |
The fluorescence spectrum of the introduced tryptophans in the alpha 3(beta F155W)3gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 cannot be used to distinguish between the number of nucleoside di- and triphosphates bound to catalytic
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Bacillus; Catalytic Domain; Mutation; Protein Subunits; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan | 2002 |
Gamma-amido-ATP stabilizes a high-fluorescence state of myosin subfragment 1.
Topics: Actomyosin; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Fluorescence; Hydrolysis; Kinetics; Myosin Subfragments; Rabbits; Temperature; Tryptophan | 2002 |
The association of actin and myosin in the presence of gamma-amido-ATP proceeds mainly via a complex with myosin in the closed conformation.
Topics: Actins; Adenosine Diphosphate; Adenylyl Imidodiphosphate; Animals; Dictyostelium; Fluorescence; Myosins; ortho-Aminobenzoates; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 2007 |