Nuclear magnetic resonance study of side-chain conformation of phenylalanine residue in [Met5]-enkephalin: Solvent, pH, and temperature dependence
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference22 articles.
1. C fragment of lipotropin has a high affinity for brain opiate receptors
2. Conformation of Met5-enkephalin determined by high field PMR spectroscopy
3. Proton magnetic resonance studies of conformation and flexibility of enkephalin peptides
4. Preferential conformation of the endogenous opiate-like pentapeptide met-enkephalin in DMSO-d6 solution determined by high field 1H NMR
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1. Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin;Magnetic Resonance in Chemistry;2014-03-18
2. NUCLEAR MAGNETIC RESONANCE STUDY ON SOLVENT DEPENDENCE OF SIDE CHAIN CONFORMATIONS OF TYROSINE AND TRYPTOPHAN DERIVATIVES;International Journal of Peptide and Protein Research;2009-01-12
3. Nuclear magnetic resonance analyses of side chain conformations of histidine and aromatic amino acid derivatives;International Journal of Peptide and Protein Research;2009-01-12
4. CONFORMATIONALSTUDY OF [LEU5]-ENKEPHALIN BY LASER RAMAN SPECTROSCOPY;International Journal of Peptide and Protein Research;2009-01-12
5. Conformational analysis of μ-selective [D-Ala2,MePhe4]enkephalins;International Journal of Peptide and Protein Research;2009-01-12
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