Neighboring Side Chain Effects on Asparaginyl and Aspartyl Degradation: An Ab Initio Study of the Relationship between Peptide Conformation and Backbone NH Acidity-Reference-Cited by-同舟云学术

Neighboring Side Chain Effects on Asparaginyl and Aspartyl Degradation: An Ab Initio Study of the Relationship between Peptide Conformation and Backbone NH Acidity

Published:2001-03-23 Issue:15 Volume:123 Page:3499-3506
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Radkiewicz Jennifer L.¹,Zipse Hendrik¹,Clarke Steven¹,Houk K. N.¹

Affiliation:

1. Contribution from the Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California 90095

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0026814

Reference45 articles.

1. Deamidation of the asparaginyl-glycyl sequence

2. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.

3. Succinimide Formation from Aspartyl and Asparaginyl Peptides as a Model for the Spontaneous Degradation of Proteins

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