The effects of a histidine (His) residue located on the C-terminal side of an asparaginyl (Asn) residue on the rate of deamidation were studied using Gly-Gln-Asn-X-His pentapeptides. The rates of deamidation of the pentapeptides were determined at 37 degrees C (I = 0.5) as function of pH, buffer spe
Effect of lysine residues on the deamidation reaction of asparagine side chains
β Scribed by Sante Capasso; Gianfranco Balboni; Paola Di Cerbo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2000
- Tongue
- English
- Weight
- 98 KB
- Volume
- 53
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
The effect of lysine residues on the deamidation reaction of the asparagine side chain has been studied on the peptide Τ½ Τ½ Ac-Cys-Lys-Asn-Gly-Gln-Thr-Asn-Cys-NH 2 and on its lysine-acetylated derivative in a wide range of pH values. The amino acid sequence of these peptides is similar to the local sequence flanking the labile Asn-67 in RNAse A. The experimental data show that Lys influences both the deamidation rate and the relative yield of the two reaction products, i.e., the aspartic acid and β€-aspartic acid containing peptide. These effects are pH dependent and can be rationalized based on the mechanism previously proposed for the deamidation reaction via succinimide derivative.
π SIMILAR VOLUMES
The conformational preferences of the monomeric units of a series of poly(a-alkylb-L-aspartate)s were examined by quantum mechanical calculations. a-Alkyl-b-aspartamyl moligopeptides with a number of residues m ranging from 1 to 7 and arranged in the conformations experimentally observed for their c