Although the conformations of two linked peptide units both with glycyl and alanyl residues have been extensively studied,'-$ no systematic investigation of the energies of conformations of two linked peptide units with side chains beyond the CB atom and a comparison with the available crystallograp
Redox Potential of Azobenzene as an Amino Acid Residue in Peptides
✍ Scribed by Cyril Boulègue; Markus Löweneck; Christian Renner; Luis Moroder
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 108 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1439-4227
No coin nor oath required. For personal study only.
✦ Synopsis
Scheme 1. Treatment of the (E)-azobenzene peptide 1 a and of its Z isomer 1 b at 25 8C in 100 mm phosphate buffer (pH 7.0) with GSH/GSSG.
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## Abstract The conformational preferences of the 3,3‐disubstituted β‐amino acid residue, 1‐aminocyclohexaneacetic acid (β^3,3^Ac~6~c) have been investigated by determining the crystal structures of the parent amino acid, the hydrochloride derivative, 10 protected derivatives and di and tripeptides
The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.