The conformational behavior of a heterodetic bicyclic decapeptide (BCPLT) in the absence and in the presence of calcium ions has been studied by means of mono and two-dimensional nmr techniques. Free BCPLT possessee a quite compact structure stabilized by intramolecular bonds and turns. In the struc
โฆ LIBER โฆ
Conformational and ion binding properties of a cyclic octapeptide, cyclo(Ala-Leu-Pro-Gly)2
โ Scribed by D. S. Seetharama Jois; K. R. K. Easwaran; Maria Bednarek; E. R. Blout
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1992
- Tongue
- English
- Weight
- 594 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0006-3525
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The cyclic hexapeptide cycle[ -Pro'-Gly2-Glu3 (OBzl) -Pro4-Phe5-Leu6-] ( 1 ; OBzl: benzyl ester) was modeled and synthesized to be used as a chiral site for the separation of enantiomers. Total correlation spectroscopy and nuclear Ovehauser effect spectroscopy spectra of the peptide in CDCIB showed