BIOFUNCTIONAL EVALUATION OF A HYDROGEN BOND STABILIZING THE β-TURN IN THE ACYCLIC PART OF OXYTOCIN
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1980.tb02934.x/fullpdf
Reference43 articles.
1. Conformational studies on [Pro3,Gly4]-oxytocin in dimethyl sulfoxide by proton nuclear magnetic resonance spectroscopy: evidence for a type II β turn in the cyclic moiety
2. THE ASSAY OF MILK-EJECTING ACTIVITY IN THE LACTATING RAT
3. Unequivocal assignments of NH proton magnetic resonance bands in oxytocin using 2 H- and 15 N-substituted molecules
4. 300-MHz Nuclear Magnetic Resonance Study of Oxytocin in Aqueous Solution: Conformational Implications
5. Carbon-13 nuclear magnetic resonance spectroscopy of oxytocin, related oligopeptides, and selected analogs
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1. Biofunctional evaluation of two hydrogen bonds stabilizing the β-turn in the acyclic component of oxytocin;International Journal of Peptide and Protein Research;2009-01-12
2. Analogs of oxytocin containing a pseudopeptide Leu-Gly bond of cis and trans configuration*;International Journal of Peptide and Protein Research;2009-01-12
3. Analogs of oxytocin containing a modified peptide bond*;International Journal of Peptide and Protein Research;2009-01-12
4. Biofunctional evaluation of a hydrogen bond stabilizing the conformation in the cyclic part of oxytocin;International Journal of Peptide and Protein Research;2009-01-12
5. Role of the carboxamide groups of the asparagine and glycinamide residues of oxytocin. Syntheses and biological properties of [5-β-cyanoalanine] oxytocin and [9-α-aminoacetonitrile] oxytocin;International Journal of Peptide and Protein Research;2009-01-12
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