In:
Bulletin of the Korean Chemical Society, Wiley, Vol. 39, No. 2 ( 2018-02), p. 244-249
Abstract:
α/β‐Peptide 11/9‐helix is an unconventional helical structure in which 11‐ and 9‐membered ring hydrogen bonds alternate along the helical axis. We have examined the interplay and the relative strength of these two hydrogen bonding types by IR, NMR, and X‐ray crystallographic methods. A pair of two adjacent hydrogen bonds with opposite directionality cooperatively stabilized each other in non‐hydrogen‐bonding solvents. In contrast, an unpaired hydrogen bond was unstable to promote helical folding. The IR and the NMR data of α/β‐depsipeptides suggested that a 9‐membered ring hydrogen bond is favored over an 11‐membered ring hydrogen bond.
Type of Medium:
Online Resource
ISSN:
1229-5949
,
1229-5949
DOI:
10.1002/bkcs.2018.39.issue-2
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
2056474-0
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