guanidine has been researched along with 1,5-i-aedans in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 8 (88.89) | 18.2507 |
| 2000's | 1 (11.11) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brand, L; James, E; Stites, W; Wu, PG | 1 |
| Hamaguchi, K; Kawata, Y | 1 |
| Dirr, H; Sluis-Cremer, N | 1 |
| Churchich, JE; Kwok, F; Kwon, OS; Lo, SC | 1 |
| Ferreira, ST; Rietveld, AW | 1 |
| Beltrán, C; Darszon, A; Ferreira, ST; Garzón-Rodríguez, W; Gómez-Puyou, A; Sepúlveda-Becerra, MA; Strasser, RJ | 1 |
| Fisher, CA; Ryan, RO | 1 |
| Abbruzzese, A; Beninati, S; Caraglia, M; Colonna, G; Hershey, JW; Ragone, R; Stiuso, P | 1 |
| Li, ZY; Zhou, JM | 1 |
9 other study(ies) available for guanidine and 1,5-i-aedans
| Article | Year |
|---|---|
Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer.
Topics: Amino Acid Sequence; Cysteine; Energy Transfer; Escherichia coli; Fluorescent Dyes; Guanidine; Guanidines; Kinetics; Lysine; Mathematics; Micrococcal Nuclease; Mutagenesis, Site-Directed; Naphthalenesulfonates; Protein Denaturation; Recombinant Proteins; Tryptophan | 1992 |
Use of fluorescence energy transfer to characterize the compactness of the constant fragment of an immunoglobulin light chain in the early stage of folding.
Topics: Circular Dichroism; Energy Transfer; Fluorescent Dyes; Guanidine; Guanidines; Immunoglobulin Light Chains; Kinetics; Naphthalenesulfonates; Protein Conformation; Spectrometry, Fluorescence; Tryptophan; X-Ray Diffraction | 1991 |
Conformational stability of Cys45-alkylated and hydrogen peroxide-oxidised glutathione S-transferase.
Topics: Alkylation; Animals; Cysteine; Dithiothreitol; Enzyme Stability; Glutathione; Glutathione Transferase; Guanidine; Guanidines; Hydrogen Peroxide; Naphthalenesulfonates; Oxidation-Reduction; Protein Conformation; Spectrometry, Fluorescence; Structure-Activity Relationship; Swine; Thermodynamics | 1995 |
Reversible unfolding of myo-inositol monophosphatase.
Topics: Animals; Brain; Cattle; Chromatography, High Pressure Liquid; Circular Dichroism; Fluorescence Polarization; Fluorescent Dyes; Guanidine; Guanidines; Hydrogen-Ion Concentration; Kinetics; Naphthalenesulfonates; Phosphoric Monoester Hydrolases; Protein Denaturation; Protein Folding; Swine | 1993 |
Deterministic pressure dissociation and unfolding of triose phosphate isomerase: persistent heterogeneity of a protein dimer.
Topics: Animals; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Guanidine; Guanidines; Kinetics; Macromolecular Substances; Muscle, Skeletal; Naphthalenesulfonates; Pressure; Protein Conformation; Protein Denaturation; Protein Folding; Rabbits; Spectrometry, Fluorescence; Thermodynamics; Triose-Phosphate Isomerase | 1996 |
Refolding of triosephosphate isomerase in low-water media investigated by fluorescence resonance energy transfer.
Topics: Animals; Cetrimonium; Cetrimonium Compounds; Cysteine; Detergents; Fluorescein-5-isothiocyanate; Guanidine; Guanidines; Hexanols; Micelles; Muscle, Skeletal; Naphthalenesulfonates; Octanes; Protein Conformation; Protein Denaturation; Protein Folding; Rabbits; Spectrometry, Fluorescence; Triose-Phosphate Isomerase | 1996 |
Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E.
Topics: Apolipoprotein E3; Apolipoproteins E; Dimyristoylphosphatidylcholine; Energy Transfer; Fluorescent Dyes; Guanidine; Humans; In Vitro Techniques; Lipid Metabolism; Micelles; Models, Molecular; Naphthalenesulfonates; Protein Binding; Protein Conformation; Recombinant Proteins; Trifluoroethanol | 1999 |
Structural organization of the human eukaryotic initiation factor 5A precursor and its site-directed variant Lys50-->Arg.
Topics: Amino Acid Substitution; Arginine; Base Sequence; Circular Dichroism; DNA Primers; Eukaryotic Translation Initiation Factor 5A; Fluorescent Dyes; Guanidine; Humans; Lysine; Mutagenesis, Site-Directed; Naphthalenesulfonates; Peptide Initiation Factors; Protein Conformation; Protein Denaturation; Protein Precursors; RNA-Binding Proteins; Spectrophotometry, Ultraviolet | 1999 |
Conformational change of dihydrofolate reductase near the active site after thiol modification: detected by limited proteolysis.
Topics: Amino Acid Sequence; Animals; Binding Sites; Chickens; Cricetinae; Cricetulus; Enzyme Activation; Female; Guanidine; Hydroxymercuribenzoates; Liver; Models, Molecular; Molecular Sequence Data; Naphthalenesulfonates; Ovary; Protein Conformation; Sulfhydryl Compounds; Sulfhydryl Reagents; Tetrahydrofolate Dehydrogenase; Trypsin | 2000 |