hydrogen has been researched along with neuropeptide y in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (60.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bernassau, JM; Cambillau, C; Chenu, J; Darbon, H; Deleuze, C; Roussel, A | 1 |
Balse, P; Chu, SS; Doughty, MB; Shobe, D; Velde, DV | 1 |
Allard, P; Arvidsson, K; Ehrenberg, A; Jarvet, J | 1 |
Bader, R; Beck-Sickinger, AG; Bettio, A; Zerbe, O | 1 |
Bader, R; Christen, B; Folkers, G; Gafner, V; Lerch, M; Zerbe, O | 1 |
5 other study(ies) available for hydrogen and neuropeptide y
Article | Year |
---|---|
Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics.
Topics: Amino Acid Sequence; Animals; Cattle; Humans; Hydrogen; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Neuropeptide Y; Pancreatic Polypeptide; Protein Conformation; Solutions | 1992 |
Conformational properties of the proline region of porcine neuropeptide Y by CD and 1H-nmr spectroscopy.
Topics: Amino Acid Sequence; Animals; Circular Dichroism; Hydrogen; Indicators and Reagents; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Neuropeptide Y; Peptide Fragments; Proline; Protein Conformation; Protein Structure, Secondary; Swine | 1995 |
Solution structure by 1H and dynamics by natural abundance 13C NMR of a receptor recognising peptide derived from a C-terminal fragment of neuropeptide Y.
Topics: Amino Acid Sequence; Animals; Carbon Isotopes; Circular Dichroism; Hydrogen; Hydrogen Bonding; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Neuropeptide Y; Peptide Fragments; Protein Structure, Tertiary; Rats; Receptors, Neuropeptide Y; Solutions; Thermodynamics; Water | 1994 |
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 |
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 |