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Cis/trans configurations of the peptide CN bonds: isomerization and photoswitching
Author(s) -
Micheau JeanClaude,
Zhao Jianzhang
Publication year - 2007
Publication title -
journal of physical organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.325
H-Index - 66
eISSN - 1099-1395
pISSN - 0894-3230
DOI - 10.1002/poc.1216
Subject(s) - chemistry , isomerization , azobenzene , thioamide , peptide bond , photochromism , photoisomerization , peptide , hydrogen bond , molecular switch , resonance (particle physics) , stereochemistry , photochemistry , crystallography , molecule , organic chemistry , catalysis , biochemistry , physics , particle physics
Abstract Cis / trans isomerization of peptide CN bonds is involved in the configurational changes and are definitive for the bioactivity of peptides and proteins. The basic molecular character and origin of the restricted rotation of the peptide CN bonds are briefly introduced, as well as the methods used for study of the cis / trans isomerization, such as the chymotrypsin‐coupled assay, pH‐mediated solvent jump, and UV‐resonance Raman spectroscopy, etc. The control of the peptide bond configuration with photoresponsive (photochromic) groups such as azobenzene or thioamide bonds is also reviewed. Copyright © 2007 John Wiley & Sons, Ltd.