Deamidation of human proteins

  1. N. E. Robinson*,† and
  2. A. B. Robinson‡
  1. *Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125; and ‡Oregon Institute of Science and Medicine, Cave Junction, OR 97523

  1. Communicated by Frederick Seitz, The Rockefeller University, New York, NY (received for review May 8, 2001)

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.

Footnotes

  • ↵ † To whom reprint requests should be addressed. E-mail: noahr{at}its.caltech.edu.

  • Abbreviation:
    3D,
    three-dimensional
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  1. Published online before print October 16, 2001, doi: 10.1073/pnas.221463198 PNAS October 23, 2001 vol. 98 no. 22 12409-12413
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