Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module

Michael Resch, Michael Himmel, Gregg Beckham, Xiaoyang Guan, Patrick Chaffey, Chen Zeng, Eric Greene, Liqun Chen, Matthew Drake, Claire Chen, Ari Groobman, Zhongping Tan

Research output: Contribution to journalArticlepeer-review

27 Scopus Citations


Protein glycosylation is a ubiquitous post-translational modification in all kingdoms of life. Despite its importance in molecular and cellular biology, the molecular-level ramifications of O-glycosylation on biomolecular structure and function remain elusive. Here, we took a small model glycoprotein and changed the glycan structure and size, amino acid residues near the glycosylation site, and glycosidic linkage while monitoring any corresponding changes to physical stability and cellulose binding affinity. The results of this study reveal the collective importance of all the studied features in controlling the most pronounced effects of O-glycosylation in this system. Going forward, this study suggests the possibility of designing proteins with multiple improved properties by simultaneously varying the structures of O-glycans and amino acids local to the glycosylation site.

Original languageAmerican English
Pages (from-to)7185-7189
Number of pages5
JournalChemical Science
Issue number12
StatePublished - 2015

Bibliographical note

Publisher Copyright:
© 2015 The Royal Society of Chemistry.

NREL Publication Number

  • NREL/JA-5100-65609


  • biomolecular structure
  • protein glycosylation


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