title: 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.
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. noahr@its.caltech.edu
authors.forename: N E
authors.initials: NE
authors.lastname: Robinson
authors.forename: A B
authors.initials: AB
authors.lastname: Robinson
mesh_terms: D001216:Asparagine / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism; D006801:Humans; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins; D005973:Glutamine; D001216:Asparagine