6-fluorotryptophan has been researched along with urea in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 1 (33.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Frieden, C; Shu, Q | 1 |
| Boyer, JA; Dalessio, PM; Ropson, IJ; Schaeffer, BA | 1 |
| Dyson, HJ; Sun, X; Wright, PE | 1 |
3 other study(ies) available for 6-fluorotryptophan and urea
| Article | Year |
|---|---|
Urea-dependent unfolding of murine adenosine deaminase: sequential destabilization as measured by 19F NMR.
Topics: Adenosine Deaminase; Animals; Circular Dichroism; Enzyme Stability; Fluorine; Magnetic Resonance Spectroscopy; Mice; Mutagenesis, Site-Directed; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan; Urea | 2004 |
Comparison of the folding mechanism of highly homologous proteins in the lipid-binding protein family.
Topics: Animals; Carrier Proteins; Humans; Hydroxysteroid Dehydrogenases; Kinetics; Membrane Glycoproteins; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Folding; Protein Structure, Secondary; Rats; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrometry, Fluorescence; Thermodynamics; Tryptophan; Tyrosine; Urea | 2009 |
Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.
Topics: Amino Acid Substitution; Dimerization; Fluorescent Dyes; Kinetics; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Prealbumin; Protein Aggregation, Pathological; Protein Conformation; Protein Denaturation; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Stability; Protein Unfolding; Recombinant Proteins; Tryptophan; Urea | 2017 |