Molecular clocks
- Creators
- Robinson, Noah E.
- Robinson, Arthur B.
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°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.
Additional Information
© 2001 National Academy of Sciences. Communicated by Bruce Merrifield, The Rockefeller University, New York, NY, November 28, 2000 (received for review September 26, 2000). We thank Professor and Mrs. R. B. Merrifield, in whose laboratory and with whose help we synthesized the peptides, and Professor Brian Chait for his advice and counsel concerning the mass spectrometry. We also thank the John Kinsman Foundation and other donors to the Oregon Institute of Science and Medicine for financial support.Attached Files
Published - PNAS-2001-Robinson-944-9.pdf
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Additional details
- PMCID
- PMC14689
- Eprint ID
- 51970
- Resolver ID
- CaltechAUTHORS:20141119-131847975
- John Kinsman Foundation
- Created
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2014-11-19Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field