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Updated: Jul 14, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Modulation of protein biophysical properties by chemical glycosylation: biochemical insights and biomedical
R J Solá1, J A Rodríguez-Martínez, K Griebenow
1Laboratory for Applied Biochemistry and Biotechnology, Department of Chemistry, University of Puerto Rico, Río Piedras Campus, Facundo Bueso Bldg., Lab-215, San Juan 23346, 00931-3346, Puerto Rico. rsola@bluebottle.com
Abstract:
Glycosylation constitutes one of the most important posttranslational modifications employed by biological systems to modulate protein biophysical properties. Due to the direct biochemical and biomedical implications of achieving control over protein stability and function by chemical means, there has been great interest in recent years towards the development of chemical strategies for protein glycosylation. Since current knowledge about glycoprotein biophysics has been mainly derived from the study of naturally glycosylated proteins, chemical glycosylation provides novel insights into its mechanistic understanding by affording control over glycosylation parameters. This review presents a survey of the effects that natural and chemical glycosylation have on the fundamental biophysical properties of proteins (structure, dynamics, stability, and function). This is complemented by a mechanistic discussion of how glycans achieve such effects and discussion of the implications of employing chemical glycosylation as a tool to exert control over protein biophysical properties within biochemical and biomedical applications.
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