Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides.
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Open Access
- 4 January 2021
- journal article
- research article
- Published by Elsevier
- Vol. 266 (33) , 22549-22556
- https://doi.org/10.1016/s0021-9258(18)54607-x
Abstract
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This publication has 36 references indexed in Scilit:
- Formation of isoaspartate 99 in bovine and porcine somatotropinsProtein Journal, 1990
- Solid-state conformations of aminosuccinyl peptides: Crystal structure oftert-butyloxycarbonyl-L-leucyl-L-aminosuccinyl-L-phenylalaninamideBiopolymers, 1989
- The unusual substrate specificity of eukaryotic protein carboxyl methyltransferasesTrends in Biochemical Sciences, 1987
- Identification of aminosuccinyl residues in peptides by second-derivative ultraviolet spectrometryPeptides, 1987
- Selective deamidation and enzymic methylation of seminal ribonucleaseBiochemistry, 1986
- Deamidation of the asparaginyl‐glycyl sequenceInternational Journal of Peptide and Protein Research, 1986
- Preferred conformations of tert.‐butyloxycarbonyl‐L‐aminosuccinyl‐glycyl‐glycine methyl ester in the solid and solution stateInternational Journal of Peptide and Protein Research, 1984
- NUCLEOPHILIC DISPLACEMENT REACTIONS AT ESTER AND THIOLESTER BONDSAnnals of the New York Academy of Sciences, 1983
- Substituent effects on amide hydrogen exchange rates in aqueous solutionJournal of the American Chemical Society, 1972
- Stereochemistry of polypeptide chain configurationsJournal of Molecular Biology, 1963