Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module
- Univ. of Colorado, Boulder, CO (United States)
- National Renewable Energy Lab. (NREL), Golden, CO (United States)
The 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. 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.
- Research Organization:
- National Renewable Energy Laboratory (NREL), Golden, CO (United States)
- Sponsoring Organization:
- USDOE Office of Energy Efficiency and Renewable Energy (EERE), Sustainable Transportation Office. Bioenergy Technologies Office (BETO)
- Grant/Contract Number:
- AC36-08GO28308
- OSTI ID:
- 1233680
- Report Number(s):
- NREL/JA-5100-65609
- Journal Information:
- Chemical Science, Vol. 6, Issue 12; Related Information: Chemical Science; ISSN 2041-6520
- Publisher:
- Royal Society of ChemistryCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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