Hydrogen bonds in the tripeptide Pro-Leu-Gly-NH217O and 1H studies
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. Chemistry and Biology of Peptides;Walter,1972
2. Solid state conformation of the C-terminal tripeptide of oxytocin, L-Pro-L-Leu-Gly-NH2.0.5H2O
3. 1H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration
4. Laser raman studies on the conformation of Pro-Leu-Gly-NH2
5. EFFECTS OF d AND l AMINO ACID RESIDUES IN LINEAR PEPTIDES ON CARBON-13 NUCLEAR MAGNETIC RESONANCE PARAMETERS
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