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

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate has been researched along with retinaldehyde in 9 studies

Research

Studies (9)

TimeframeStudies, this research(%)All Research%
pre-19901 (11.11)18.7374
1990's5 (55.56)18.2507
2000's2 (22.22)29.6817
2010's1 (11.11)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bennett, RR; Brown, PK1
Booth, PJ; Flitsch, SL; Greenhalgh, DA; Khorana, HG; Kim, PS; Stern, LJ1
Dickerson, CD; Osawa, S; Shi, W; Weiss, ER1
Mukohata, Y; Sugiyama, Y1
Booth, PJ; Chadborn, N; Curran, AR; Farooq, A; Flitsch, SL; Riley, ML; Templer, RH; Wright, P1
Booth, PJ; Farooq, A1
Allen, SJ; Booth, PJ; Khorana, HG; Kim, JM1
Allen, SJ; Booth, PJ; Khorana, HG; Kim, JM; Lu, H1
Huber, T; Sakmar, TP; Tian, H1

Other Studies

9 other study(ies) available for 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and retinaldehyde

ArticleYear
Properties of the visual pigments of the moth Manduca sexta and the effects of two detergents, digitonin and chaps.
    Vision research, 1985, Volume: 25, Issue:12

    Topics: Animals; Cholic Acids; Detergents; Digitonin; Female; Kinetics; Lepidoptera; Light; Male; Moths; Retinal Pigments; Retinaldehyde; Solutions; Spectrophotometry; Surface-Active Agents

1985
Intermediates in the folding of the membrane protein bacteriorhodopsin.
    Nature structural biology, 1995, Volume: 2, Issue:2

    Topics: Apoproteins; Bacteriorhodopsins; Cholic Acids; Detergents; Dimyristoylphosphatidylcholine; Membrane Proteins; Micelles; Models, Molecular; Protein Binding; Protein Folding; Retinaldehyde; Schiff Bases; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence

1995
Effects of carboxyl-terminal truncation on the stability and G protein-coupling activity of bovine rhodopsin.
    Biochemistry, 1994, Jun-21, Volume: 33, Issue:24

    Topics: Amino Acid Sequence; Animals; Cattle; Cell Line; Cell Membrane; Cholic Acids; DNA, Complementary; Drug Stability; Gene Expression; Glycosylation; GTP-Binding Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphorylation; Point Mutation; Retinaldehyde; Rhodopsin; Structure-Activity Relationship; Transfection

1994
Dual roles of DMPC and CHAPS in the refolding of bacterial opsins in vitro.
    Journal of biochemistry, 1996, Volume: 119, Issue:6

    Topics: Apoproteins; Bacteriorhodopsins; Cholic Acids; Circular Dichroism; Detergents; Dimyristoylphosphatidylcholine; Halobacterium; Pigments, Biological; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Retinaldehyde; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

1996
Evidence that bilayer bending rigidity affects membrane protein folding.
    Biochemistry, 1997, Jan-07, Volume: 36, Issue:1

    Topics: Bacteriorhodopsins; Cholic Acids; Dimyristoylphosphatidylcholine; Hydrogen-Ion Concentration; Kinetics; Lipid Bilayers; Liposomes; Membrane Proteins; Models, Chemical; Phospholipid Ethers; Protein Folding; Retinaldehyde; Spectrometry, Fluorescence; Spectrophotometry; Thermodynamics

1997
Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy.
    European journal of biochemistry, 1997, Jun-15, Volume: 246, Issue:3

    Topics: Bacteriorhodopsins; Cholic Acids; Detergents; Kinetics; Light; Micelles; Protein Folding; Retinaldehyde; Scattering, Radiation; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Spectrophotometry, Atomic; Time Factors

1997
Structure and function in bacteriorhodopsin: the role of the interhelical loops in the folding and stability of bacteriorhodopsin.
    Journal of molecular biology, 2001, Apr-27, Volume: 308, Issue:2

    Topics: Amino Acid Sequence; Bacteriorhodopsins; Cholic Acids; Dimyristoylphosphatidylcholine; Halobacterium salinarum; Hydroxylamine; Ion Transport; Kinetics; Light; Micelles; Models, Molecular; Molecular Sequence Data; Phospholipid Ethers; Protein Denaturation; Protein Engineering; Protein Folding; Protein Structure, Secondary; Protons; Recombinant Proteins; Retinaldehyde; Sodium Dodecyl Sulfate; Spectrum Analysis; Structure-Activity Relationship; Thermodynamics

2001
Structure and function in bacteriorhodopsin: the effect of the interhelical loops on the protein folding kinetics.
    Journal of molecular biology, 2001, Apr-27, Volume: 308, Issue:2

    Topics: Apoproteins; Bacteriorhodopsins; Cholic Acids; Dimyristoylphosphatidylcholine; Fluorescence; Halobacterium salinarum; Kinetics; Micelles; Mutation; Phospholipid Ethers; Protein Folding; Protein Renaturation; Retinaldehyde; Sodium Dodecyl Sulfate; Spectrum Analysis; Structure-Activity Relationship; Thermodynamics

2001
The Energetics of Chromophore Binding in the Visual Photoreceptor Rhodopsin.
    Biophysical journal, 2017, Jul-11, Volume: 113, Issue:1

    Topics: Animals; Calorimetry; Cattle; Cholic Acids; Dynamic Light Scattering; Fluorescence Resonance Energy Transfer; Hydrodynamics; Kinetics; Lipid Bilayers; Micelles; Phosphatidylcholines; Photobleaching; Protein Binding; Protein Stability; Receptors, Adrenergic, beta; Retinaldehyde; Rhodopsin; Thermodynamics; Water

2017