| Literature DB >> 10595558 |
A A Kosky1, U O Razzaq, M J Treuheit, D N Brems.
Abstract
Asn deamidation was monitored in Ala-based octadecapeptides of varying alpha-helicity. Gly was substituted for Ala residues at positions 6 and 16 to create a peptide with less helicity. Ala --> Gly substitutions were made at three or more residues from the Asn to negate known primary sequence effects on deamidation rates. The extent of helicity and rate of Asn deamidation for alkaline aqueous solutions of each peptide was measured as a function of temperature by circular dichroism and reversed-phase high-performance liquid chromatography, respectively. The rate of deamidation in the peptides was inversely proportional to the extent of alpha-helicity. The results support the conclusion that Asn deamidation only occurs in the nonhelical population of conformers.Entities:
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Year: 1999 PMID: 10595558 PMCID: PMC2144212 DOI: 10.1110/ps.8.11.2519
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725