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3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and deuterium

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate has been researched along with deuterium in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's3 (60.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Horne, WA; Oswald, RE; Weiland, GA1
Davies, J; Riechmann, L1
Anglister, J; Bax, A; Grzesiek, S; Klee, CB; Ren, H; Wang, AC1
Alcántara, R; Aragón, C; López-Corcuera, B; Vázquez, J1
Battiste, JL; Wagner, G1

Other Studies

5 other study(ies) available for 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and deuterium

ArticleYear
Solubilization and hydrodynamic characterization of the dihydropyridine receptor from rat ventricular muscle.
    The Journal of biological chemistry, 1986, Mar-15, Volume: 261, Issue:8

    Topics: Animals; Calcium Channels; Centrifugation, Density Gradient; Cholic Acids; Chromatography, Gel; Deuterium; Deuterium Oxide; Digitonin; Male; Molecular Weight; Myocardium; Octoxynol; Polyethylene Glycols; Polysorbates; Rats; Rats, Inbred Strains; Receptors, Nicotinic; Solubility; Water

1986
'Camelising' human antibody fragments: NMR studies on VH domains.
    FEBS letters, 1994, Feb-21, Volume: 339, Issue:3

    Topics: Amino Acid Sequence; Animals; Base Sequence; Camelus; Cholic Acids; Deuterium; Drug Stability; Escherichia coli; Humans; Immunoglobulin Heavy Chains; Immunoglobulin Variable Region; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Sequence Homology

1994
1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B.
    Biochemistry, 1994, Mar-29, Volume: 33, Issue:12

    Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Calcineurin; Calcium; Calmodulin-Binding Proteins; Cholic Acids; Deuterium; Humans; Hydrogen; Macromolecular Substances; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Phosphoprotein Phosphatases; Protein Structure, Secondary

1994
Hydrodynamic properties and immunological identification of the sodium- and chloride-coupled glycine transporter.
    The Journal of biological chemistry, 1993, Jan-25, Volume: 268, Issue:3

    Topics: Amino Acid Transport Systems, Neutral; Animals; Antigens; Brain Stem; Carrier Proteins; Centrifugation, Density Gradient; Chemical Phenomena; Chemistry, Physical; Chlorides; Cholic Acid; Cholic Acids; Chromatography, Gel; Deuterium; Glycine Plasma Membrane Transport Proteins; Immune Sera; Immunosorbent Techniques; Molecular Weight; Sodium; Swine

1993
Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data.
    Biochemistry, 2000, May-09, Volume: 39, Issue:18

    Topics: Amino Acid Sequence; Cholic Acids; Deuterium; Eukaryotic Initiation Factor-4E; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Nitrogen Isotopes; Peptide Initiation Factors; Protein Folding; Protein Structure, Secondary; Proteins; Spin Labels; Yeasts

2000