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Stereochemistry of α-aminoisobutyric acid peptides in solution: Conformations of decapeptides with a central triplet of contiguous L-amino acids

✍ Scribed by Hemalatha Balaram; M. Sukumar; P. Balaram

Publisher
Wiley (John Wiley & Sons)
Year
1986
Tongue
English
Weight
839 KB
Volume
25
Category
Article
ISSN
0006-3525

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✦ Synopsis

270-MHz' H-nmr. In CDCl,, the presence of eight intramolecularly hydrogen-bonded N H groups has been established, consistent with a 3,,,-helical conformation, for both decapeptides. In (CD,),SO, only seven solvent-shielded NH groups are observed, supporting either an a-helical conformation or a partially unfolded 3,0-helix. Ir studies provided supporting evidence for intramolecularly hydrogen-bonded structures in CHCI,, while CD studies suggest helical conformation in both decapeptides in various solvents. CD studies also support helical folding in the C-terminal hexapeptides. The central triplet of L-amino acids appears to destabilize 3,0-helical conformations in polar solvents like (CD,),SO.

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## Abstract The ^13^C chemical shifts and spin‐lattice relaxation times are reported for __cyclo__(L‐Pro‐L‐Leu) and __cyclo__(L‐Pro‐D‐Leu). The chemical shifts of the D and L leucyl residues in the cyclic peptides differ from each other by 1.8 and 3.6 parts per million for the α and β carbons, resp