hydrogen has been researched along with dodecylphosphocholine in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (12.50) | 18.7374 |
| 1990's | 4 (50.00) | 18.2507 |
| 2000's | 3 (37.50) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Boelens, R; de Haas, G; Dekker, N; Dijkman, R; Kaptein, R; Peters, AR; Slotboom, AJ | 1 |
| Braun, W; Lee, KH; Wider, G; Wüthrich, K | 1 |
| Gesell, J; Opella, SJ; Zasloff, M | 1 |
| Fregeau Gallagher, NL; Nakashima, TT; Niemczura, WP; Sailer, M; Stiles, ME; Vederas, JC | 1 |
| Bechinger, B; Kinder, R; Mattila, K | 1 |
| Bader, R; Beck-Sickinger, AG; Bettio, A; Zerbe, O | 1 |
| Arseniev, AS; Balashova, TA; Efremov, RG; Ovchinnikova, TV; Raap, J; Shenkarev, ZO; Yakimenko, ZA | 1 |
| Bader, R; Christen, B; Folkers, G; Gafner, V; Lerch, M; Zerbe, O | 1 |
8 other study(ies) available for hydrogen and dodecylphosphocholine
| Article | Year |
|---|---|
Two-dimensional 1H-NMR studies of phospholipase-A2-inhibitor complexes bound to a micellar lipid-water interface.
Topics: Animals; Binding Sites; Binding, Competitive; Hydrogen; Magnetic Resonance Spectroscopy; Micelles; Pancreas; Phospholipases A; Phospholipases A2; Phospholipids; Phosphorylcholine; Protein Conformation; Swine; Water | 1991 |
Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
Topics: Amino Acid Sequence; Glucagon; Hydrogen; Magnetic Resonance Spectroscopy; Micelles; Models, Chemical; Phosphorylcholine; Protein Conformation; Water | 1983 |
Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.
Topics: Amino Acid Sequence; Anti-Infective Agents; Antimicrobial Cationic Peptides; Deuterium; Hydrogen; Magainins; Magnetic Resonance Spectroscopy; Micelles; Models, Molecular; Molecular Sequence Data; Peptides; Phosphorylcholine; Protein Structure, Secondary; Sodium Dodecyl Sulfate; Solutions; Trifluoroethanol; Water; Xenopus Proteins | 1997 |
Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria.
Topics: Amino Acid Sequence; Bacteriocins; Circular Dichroism; Hydrogen; Lactobacillus; Magnetic Resonance Spectroscopy; Micelles; Molecular Sequence Data; Phosphorylcholine; Protein Conformation; Sequence Homology, Amino Acid; Trifluoroethanol | 1997 |
The alignment of a voltage-sensing peptide in dodecylphosphocholine micelles and in oriented lipid bilayers by nuclear magnetic resonance and molecular modeling.
Topics: Amino Acid Sequence; Animals; Anisotropy; Carbon Tetrachloride; Computer Simulation; Electric Conductivity; Hydrogen; Lipid Bilayers; Micelles; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Phosphorylcholine; Protons; Rats; Sodium Channels; Solutions; Spin Labels; Water | 1999 |
Structure and dynamics of micelle-bound neuropeptide Y: comparison with unligated NPY and implications for receptor selection.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cell Membrane; Circular Dichroism; Dimerization; Hydrogen; Kinetics; Ligands; Micelles; Models, Biological; Models, Molecular; Molecular Mimicry; Molecular Sequence Data; Neuropeptide Y; Nuclear Magnetic Resonance, Biomolecular; Phosphorylcholine; Pliability; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Neuropeptide Y; Solutions; Spin Labels; Structure-Activity Relationship; Substrate Specificity; Swine; Thermodynamics | 2001 |
Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating.
Topics: Anisotropy; Anti-Bacterial Agents; Cell Membrane; Databases as Topic; Hydrogen; Hydrogen-Ion Concentration; Ion Channels; Lipid Bilayers; Magnetic Resonance Spectroscopy; Micelles; Peptaibols; Peptides; Phosphorylcholine; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrophotometry; Temperature; Time Factors | 2002 |
Bovine pancreatic polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles.
Topics: Animals; Cattle; Humans; Hydrogen; Micelles; Models, Molecular; Neuropeptide Y; Nuclear Magnetic Resonance, Biomolecular; Pancreatic Polypeptide; Phosphorylcholine; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Solutions; Spin Labels; Structure-Activity Relationship | 2002 |