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Cooperative Effect of the Two Hydrogen Bonding Types on 11/9‐Helical Folding of α/β‐Peptides
Author(s) -
Jang Geunhyuk,
Lee Mihye,
Lee Jaeyeon,
Shim Jihyun,
Kang Philjae,
Choi MoonGun,
Choi Soo Hyuk
Publication year - 2018
Publication title -
bulletin of the korean chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.237
H-Index - 59
ISSN - 1229-5949
DOI - 10.1002/bkcs.11376
Subject(s) - hydrogen bond , ring (chemistry) , folding (dsp implementation) , chemistry , crystallography , low barrier hydrogen bond , helix (gastropod) , beta sheet , protein folding , hydrogen , stereochemistry , peptide , molecule , organic chemistry , biochemistry , snail , electrical engineering , biology , engineering , ecology
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.