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Cis/trans configurations of the peptide C-N bonds: isomerization and photoswitching
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Indexed by:期刊论文

Date of Publication:2007-11-01

Journal:Japanese-French Joint Seminar on Organic Photochromism-Switches and Memories

Included Journals:SCIE、CPCI-S

Volume:20

Issue:11

Page Number:810-820

ISSN No.:0894-3230

Key Words:cis/trans isomerization; rotation barrier; peptide thioamide bond; peptidyl-prolyl bond; azobenzene; photoswitching; photoresponsiveness

Abstract:Cis/trans isomerization of peptide C-N 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 C-N 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 (c) 2007 John Wiley & Sons, Ltd.

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Gender:Male

Alma Mater:Jilin University

Degree:Doctoral Degree

School/Department:School of Chemistry Engineering

Discipline:Organic Chemistry. Applied Chemistry. Physical Chemistry (including Chemical Physics)

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