hydrogen has been researched along with egg white in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (36.36) | 18.7374 |
| 1990's | 6 (54.55) | 18.2507 |
| 2000's | 1 (9.09) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hallenga, K; Koenig, SH; Shporer, M | 1 |
| Dinh, A; Gregory, RB; Rosenberg, A | 1 |
| Levitt, M | 1 |
| McBride-Warren, PA; Mueller, DD | 1 |
| Hünenberger, PH; Mark, AE; van Gunsteren, WF | 1 |
| Kawano, K; Nagadome, H; Terada, Y | 1 |
| Buck, M; Dobson, CM; Radford, SE | 1 |
| Benjamin, DC; Poljak, RJ; Rule, GS; Williams, DC | 1 |
| Balaram, P; Bhattacharjya, S | 1 |
| Connolly, PJ; Klibanov, AM; Knubovets, T; Osterhout, JJ | 1 |
| Vogtt, K; Winter, R | 1 |
11 other study(ies) available for hydrogen and egg white
| Article | Year |
|---|---|
Protein-water interaction studied by solvent 1H, 2H, and 17O magnetic relaxation.
Topics: Animals; Binding Sites; Chickens; Deuterium; Egg White; Helix, Snails; Hemocyanins; Hydrogen; Kinetics; Magnetic Resonance Spectroscopy; Mathematics; Molecular Weight; Muramidase; Oxygen Isotopes; Protein Binding; Protein Conformation; Proteins; Water | 1975 |
The effect of tri-N-acetylglucosamine on hydrogen exchange in hen egg white lysozyme.
Topics: Acetylglucosamine; Animals; Binding Sites; Chickens; Egg White; Glucosamine; Hydrogen; Mathematics; Models, Molecular; Muramidase; Polymers; Protein Conformation | 1986 |
Energy refinement of hen egg-white lysozyme.
Topics: Animals; Chickens; Computers; Cyclohexanes; Egg White; Electrons; Hydrogen; Muramidase; Protein Conformation; Spectrum Analysis; X-Ray Diffraction | 1974 |
Hydrogen-deuterium exchange of lysozyme. I. Rate constants and pH dependence.
Topics: Animals; Chemical Phenomena; Chemistry; Chickens; Computers; Deuterium; Egg White; Hydrogen; Hydrogen-Ion Concentration; Infrared Rays; Kinetics; Mathematics; Muramidase; Protein Conformation; Spectrophotometry | 1972 |
Computational approaches to study protein unfolding: hen egg white lysozyme as a case study.
Topics: Amides; Animals; Chemical Phenomena; Chemistry, Physical; Chickens; Computer Simulation; Egg White; Female; Hydrogen; Kinetics; Models, Molecular; Muramidase; Pressure; Protein Folding; Temperature; Water | 1995 |
Identification of the adsorbing site of lysozyme onto the hydroxyapatite surface using hydrogen exchange and 1H NMR.
Topics: Adsorption; Animals; Chickens; Durapatite; Egg White; Hydrogen; Hydroxyapatites; Magnetic Resonance Spectroscopy; Muramidase; Protein Conformation | 1993 |
A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding.
Topics: Amino Acid Sequence; Animals; Chickens; Circular Dichroism; Egg White; Female; Hydrogen; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Muramidase; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Trifluoroethanol | 1993 |
Reduction in the amide hydrogen exchange rates of an anti-lysozyme Fv fragment due to formation of the Fv-lysozyme complex.
Topics: Amides; Animals; Antibodies, Monoclonal; Antigen-Antibody Complex; Bromosuccinimide; Egg White; Hydrogen; Immunoglobulin Fragments; Magnetic Resonance Spectroscopy; Models, Molecular; Muramidase; Oxidation-Reduction; Protein Conformation | 1997 |
Effects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide.
Topics: Animals; Chickens; Circular Dichroism; Deuterium; Dimethyl Sulfoxide; Egg White; Fluorescence; Hydrogen; Magnetic Resonance Spectroscopy; Models, Molecular; Muramidase; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Solvents; Temperature; Ultraviolet Rays; Water | 1997 |
Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol.
Topics: Animals; Chickens; Circular Dichroism; Egg White; Enzyme Stability; Glycerol; Hot Temperature; Hydrogen; Models, Molecular; Muramidase; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Denaturation; Protein Conformation; Protein Structure, Secondary; Thermodynamics; Water | 1999 |
Pressure-assisted cold denaturation of hen egg white lysozyme: the influence of co-solvents probed by hydrogen exchange nuclear magnetic resonance.
Topics: Animals; Chickens; Cold Temperature; Egg White; Hot Temperature; Hydrogen; Hydrostatic Pressure; Magnetic Resonance Imaging; Muramidase; Protein Denaturation; Solvents; Sorbitol; Urea | 2005 |