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PMID: 11158575 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular clocks.

Robinson NE, Robinson AB

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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20 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2001-01-30
Pages
944-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC14689
Subset
IM
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