Publication | Open Access
Deamidation of human proteins
280
Citations
32
References
2001
Year
Protein ChemistryAsparaginyl ResiduesProtein FunctionBiochemistryProtein AssemblyProtein FoldingNatural SciencesPeptide LibraryHuman ProteinsMolecular BiologyDeamidation RatesProtein EngineeringChemical BiologyProteomicsProtein DegradationProtein Purification
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.
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