Abstract
A convenient and precise mass spectrometric method for measurement of the deamidation rates of glutaminyl and asparaginyl residues in peptides and proteins has been developed; the rates of deamidation of 306 asparaginyl sequences in model peptides at pH 7.4, 37.0 degrees C, 0.15 M Tris.HCl buffer have been determined; a library of 913 amide-containing peptides for use by other investigators in similar studies has been established; and, by means of simultaneous deamidation rate measurements of rabbit muscle aldolase and appropriate model peptides in the same solutions, the use of this method for quantitative measurement of the relative effects of primary, secondary, tertiary, and quaternary protein structure on deamidation rates has been demonstrated. The measured rates are discussed with respect to the hypothesis that glutaminyl and asparaginyl residues serve, through deamidation, as molecular timers of biological events.
MeSH Terms
Amides
Amino Acid Sequence
Animals
Biological Clocks
Fructose-Bisphosphate Aldolase/chemistry,metabolism
Indicators and Reagents
Kinetics
Mass Spectrometry
Models, Biological
Muscle, Skeletal/enzymology
Oligopeptides/chemical synthesis,chemistry
Peptide Fragments/chemical synthesis,chemistry
Peptide Library
Rabbits
Chemicals
Amides
Indicators and Reagents
Oligopeptides
Peptide Fragments
Peptide Library
Fructose-Bisphosphate Aldolase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Robinson N E
Department of Chemistry, California Institute of Technology, Pasadena, CA 91125, USA.
Robinson A B
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