Published December 20, 1993
| public
Book Section - Chapter
Investigation of the Origins of Specificity and Reactivity in N-Linked Protein Glycosylation
- Creators
- Imperiali, B.
- Rickert, K. W.
Abstract
Post and co-translational protein processing reactions show a broad range of both specificity and reactivity. One such reaction, asparagine linked glycosylation, is specific for Asn-Xaa-Thr/Ser sequences and is interesting for the remarkable reactivity shown by the asparagine sidechain nitrogen. The effects of the substrate conformation are examined, and it is found that the ability to form an Asx-turn is important for the peptide to undergo glycosylation. The mechanism by which the reactivity of the asparagine is increased is investigated by examining the binding properties of a series of peptides containing asparagine analogs. A model mechanism, consistent with the observed results, is proposed.
Additional Information
© 1994 American Chemical Society. Received April 30, 1993. Published in print 20 December 1993. This work was supported by the NIH (GM39334) and Sterling Drug Inc. In addition we gratefully acknowledge the award of a Fannie and John Hertz Foundation Fellowship to K.W.R.Additional details
- Eprint ID
- 85657
- Resolver ID
- CaltechAUTHORS:20180405-150603319
- GM39334
- NIH
- Sterling Drug Inc.
- Fannie and John Hertz Foundation
- Created
-
2018-04-05Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field
- Series Name
- ACS Symposium Series
- Series Volume or Issue Number
- 551