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Conformational implications of asparagine-linked glycosylation

Imperiali, Barbara and Rickert, Keith W. (1995) Conformational implications of asparagine-linked glycosylation. Proceedings of the National Academy of Sciences of the United States of America, 92 (1). pp. 97-101. ISSN 0027-8424. PMCID PMC42824. doi:10.1073/pnas.92.1.97.

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The effects of cotranslational protein modification on the process of protein folding are poorly understood. Time-resolved fluorescence energy transfer has been used to assess the impact of glycosylation on the conformational dynamics of flexible oligopeptides. The peptide sequences examined are selected from glycoproteins of known three-dimensional structure. The energy transfer modulation associated with N-linked glycosylation is consistent with the glycopeptides sampling different conformational profiles in water. Results show that glycosylation causes the modified peptides to adopt a different ensemble of conformations, and for some peptides this change may lead to conformations that are more compact and better approximate the conformation of these peptides in the final folded protein. This result further implies that cotranslational glycosylation can trigger the timely formation of structural nucleation elements and thus assist in the complex process of protein folding.

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Additional Information:© 1995 National Academy of Sciences. Communicated by Peter B. Dervan, California Institute of Technology, Pasadena, CA, September 20, 1994 (received for review June 23, 1994). We are grateful to Chris Kenyon and Dr. Jay Winkler of the Beckman Institute Laser Resource Center for the use of the time-correlated single-photon-counting apparatus and for invaluable technical assistance. The Laser Resource Center is supported by the Arnold and Mabel Beckman Foundation. This research was supported by National Institutes of Health grant GM 39334 and a Fannie and John Hertz predoctoral fellowship (to K.W.R.). B.I. also acknowledges support from the Alfred P. Sloan Foundation, the Camille and Henry Dreyfus Teacher Scholar Program, the Lilly Grantee Program, and Zeneca Pharmaceuticals. This paper is contribution no. 8981 from the Division of Chemistry and Chemical Engineering, California Institute of Technology. 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.
Funding AgencyGrant Number
Arnold and Mabel Beckman FoundationUNSPECIFIED
NIHGM 39334
Fannie and John Hertz FoundationUNSPECIFIED
Alfred P. Sloan FoundationUNSPECIFIED
Camille and Henry Dreyfus FoundationUNSPECIFIED
Zeneca PharmaceuticalsUNSPECIFIED
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Caltech Division of Chemistry and Chemical Engineering8981
Issue or Number:1
PubMed Central ID:PMC42824
Record Number:CaltechAUTHORS:20141205-093641933
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Official Citation:B Imperiali and K W Rickert Conformational implications of asparagine-linked glycosylation PNAS 1995 92 (1) 97-101
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52428
Deposited By: Tony Diaz
Deposited On:09 Dec 2014 22:52
Last Modified:10 Nov 2021 19:40

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