Unknown

Dataset Information

0

Deamidation of human proteins.


ABSTRACT: Deamidation of asparaginyl and glutaminyl residues causes time-dependent changes in charge and conformation of peptides and proteins. Quantitative and experimentally verified predictive calculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 126 human proteins have been performed. These rates suggest that deamidation is a biologically relevant phenomenon in a remarkably large percentage of human proteins.

SUBMITTER: Robinson NE 

PROVIDER: S-EPMC60067 | biostudies-literature | 2001 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Deamidation of human proteins.

Robinson N E NE   Robinson A B AB  

Proceedings of the National Academy of Sciences of the United States of America 20011016 22


Deamidation of asparaginyl and glutaminyl residues causes time-dependent changes in charge and conformation of peptides and proteins. Quantitative and experimentally verified predictive calculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 126 human proteins have been performed. These rates suggest that deamidation is a biologically relevant phenomenon in a remarkably large percentage of human proteins. ...[more]

Similar Datasets

| S-EPMC2678484 | biostudies-literature
| S-EPMC3202810 | biostudies-literature
| S-EPMC8032661 | biostudies-literature
| S-EPMC2533042 | biostudies-literature
| S-EPMC122761 | biostudies-literature
| S-EPMC5515959 | biostudies-literature
| S-EPMC5760270 | biostudies-literature
| S-EPMC2597435 | biostudies-literature
| S-EPMC4401446 | biostudies-literature
| S-EPMC7096717 | biostudies-literature