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2-(4-toluidino)-6-naphthalenesulfonic acid and urea

2-(4-toluidino)-6-naphthalenesulfonic acid has been researched along with urea in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19901 (25.00)18.7374
1990's2 (50.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bruice, TC; Massey, V; Schopfer, LM; Wessiak, A; Yuan, LC1
Fan, YX; Ju, M; Tsou, CL; Zhou, JM1
DiNardo, AA; Merrill, AR; Steer, BA1
Qin, SB; Zhang, HJ; Zhang, WH; Zhu, ZY1

Other Studies

4 other study(ies) available for 2-(4-toluidino)-6-naphthalenesulfonic acid and urea

ArticleYear
Use of riboflavin-binding protein to investigate steric and electronic relationships in flavin analogs and models.
    Proceedings of the National Academy of Sciences of the United States of America, 1984, Volume: 81, Issue:14

    Topics: Binding Sites; Carrier Proteins; Flavins; Hydantoins; Kinetics; Membrane Transport Proteins; Models, Chemical; Naphthalenesulfonates; Pteridines; Spiro Compounds; Stereoisomerism; Structure-Activity Relationship; Urea

1984
Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site.
    The Biochemical journal, 1996, Apr-01, Volume: 315 ( Pt 1)

    Topics: Amino Acid Sequence; Animals; Binding Sites; Chickens; Enzyme Activation; Fluorescence; Fluorescent Dyes; Guanidine; Guanidines; Liver; Mice; Molecular Sequence Data; Naphthalenesulfonates; Peptide Fragments; Protein Conformation; Protein Denaturation; Solutions; Tetrahydrofolate Dehydrogenase; Trypsin; Urea

1996
Colicin E1 forms a dimer after urea-induced unfolding.
    The Biochemical journal, 1999, Jun-15, Volume: 340 ( Pt 3)

    Topics: Amino Acid Sequence; Amino Acid Substitution; Chromatography, High Pressure Liquid; Circular Dichroism; Colicins; Dimerization; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Guanidine; Models, Molecular; Molecular Sequence Data; Naphthalenesulfonates; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Tryptophan; Urea

1999
Sequential conformation changes of chinese hamster ovary dihydrofolate reductase at its active sites.
    Protein and peptide letters, 2005, Volume: 12, Issue:5

    Topics: Animals; Binding Sites; CHO Cells; Cricetinae; Cricetulus; Fluorescent Dyes; Models, Theoretical; NADP; Naphthalenesulfonates; Protein Conformation; Protein Folding; Tetrahydrofolate Dehydrogenase; Urea

2005