Infrared absorption study of human proinsulin C-peptide fragments in dichloromethane.
作者： Mitsuaki Narita , Toshihiko Ogura , Kazuhiro Sato , Shinya Honda
DOI: 10.1246/BCSJ.59.2445
关键词:
摘要: In connection with the relationship between conformation and solubility of peptide intermediates having polar side chains, IR spectroscopic conformational analysis human proinsulin C-peptide fragments was performed in dichloromethane. The amino acid residues involved are Glu(OBzl), Asp(OBzl), Gin, Ser(Bzl). Especially, N–H stretching absorption spectra have been explored over a wide range concentration. Based on concentration dependence bands, it has shown that characteristic band around 3330 cm−1 is due to intramolecular hydrogen bond. Intermolecular bonding also occurs small extent these peptides, giving rise slight bands. Conformational behaviors oligopeptides protected chains Glu(OBzl) Asp(OBzl) just same as those corresponding homooligo(Leu)s, indicating pol...
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