3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate has been researched along with retinaldehyde in 9 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (11.11) | 18.7374 |
1990's | 5 (55.56) | 18.2507 |
2000's | 2 (22.22) | 29.6817 |
2010's | 1 (11.11) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bennett, RR; Brown, PK | 1 |
Booth, PJ; Flitsch, SL; Greenhalgh, DA; Khorana, HG; Kim, PS; Stern, LJ | 1 |
Dickerson, CD; Osawa, S; Shi, W; Weiss, ER | 1 |
Mukohata, Y; Sugiyama, Y | 1 |
Booth, PJ; Chadborn, N; Curran, AR; Farooq, A; Flitsch, SL; Riley, ML; Templer, RH; Wright, P | 1 |
Booth, PJ; Farooq, A | 1 |
Allen, SJ; Booth, PJ; Khorana, HG; Kim, JM | 1 |
Allen, SJ; Booth, PJ; Khorana, HG; Kim, JM; Lu, H | 1 |
Huber, T; Sakmar, TP; Tian, H | 1 |
9 other study(ies) available for 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and retinaldehyde
Article | Year |
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Properties of the visual pigments of the moth Manduca sexta and the effects of two detergents, digitonin and chaps.
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.
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.
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.
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.
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.
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.
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.
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.
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 |