Published October 23, 2001
| Version Published
Journal Article
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Deamidation of human proteins
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.
Additional Information
© 2001 National Academy of Sciences. Communicated by Frederick Seitz, The Rockefeller University, New York, NY, August 31, 2001 (received for review May 8, 2001). Published ahead of print October 16, 2001. We thank Professor and Mrs. R. B. Merrifield for advice and encouragement, and the Kinsman foundation and other donors to the Oregon Institute of Science and Medicine for financial support. Additional information is available at www.deamidation.org. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - PNAS-2001-Robinson-12409-13.pdf
Files
PNAS-2001-Robinson-12409-13.pdf
Additional details
Identifiers
- PMCID
- PMC60067
- Eprint ID
- 51973
- Resolver ID
- CaltechAUTHORS:20141119-132604985
Funding
- John Kinsman Foundation
Dates
- 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