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

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.
 [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [1] ;  [2] ;  [2] ;  [2] ;  [1]
  1. Univ. of Colorado, Boulder, CO (United States)
  2. National Renewable Energy Lab. (NREL), Golden, CO (United States)
Publication Date:
Report Number(s):
Journal ID: ISSN 2041-6520
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Chemical Science
Additional Journal Information:
Journal Volume: 6; Journal Issue: 12; Related Information: Chemical Science; Journal ID: ISSN 2041-6520
Royal Society of Chemistry
Research Org:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Bioenergy Technologies Office (EE-3B)
Country of Publication:
United States
09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; protein glycosylation; biomolecular structure
OSTI Identifier: