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Published April 10, 2001 | Published
Journal Article Open

Prediction of protein deamidation rates from primary and three-dimensional structure

Abstract

A method for the quantitative estimation of instability with respect to deamidation of the asparaginyl (Asn) residues in proteins is described. The procedure involves the observation of several simple aspects of the three-dimensional environment of each Asn residue in the protein and a calculation that includes these observations, the primary amino acid residue sequence, and the previously reported complete set of sequence-dependent rates of deamidation for Asn pentapeptides. This method is demonstrated and evaluated for 23 proteins in which 31 unstable and 167 stable Asn residues have been reported and for 7 unstable and 63 stable Asn residues that have been reported in 61 human hemoglobin variants. The relative importance of primary structure and three-dimensional structure in Asn deamidation is estimated.

Additional Information

© 2001 National Academy of Sciences. Communicated by Bruce Merrifield, The Rockefeller University, New York, NY, February 8, 2001 (received for review January 13, 2001). We thank Prof. and Mrs. R. B. Merrifield for their advice and encouragement. We also thank the John Kinsman Foundation and other donors to the Oregon Institute of Science and Medicine for financial support.

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August 21, 2023
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