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

Abstract

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.

Authors:
 [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:
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)
OSTI Identifier:
1233680
Report Number(s):
NREL/JA-5100-65609
Journal ID: ISSN 2041-6520
Grant/Contract Number:  
AC36-08GO28308
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Chemical Science
Additional Journal Information:
Journal Volume: 6; Journal Issue: 12; Related Information: Chemical Science; Journal ID: ISSN 2041-6520
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; protein glycosylation; biomolecular structure

Citation Formats

Guan, Xiaoyang, Chaffey, Patrick K., Zeng, Chen, Greene, Eric R., Chen, Liqun, Drake, Matthew R., Chen, Claire, Groobman, Ari, Resch, Michael G., Himmel, Michael E., Beckham, Gregg T., and Tan, Zhongping. Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module. United States: N. p., 2015. Web. doi:10.1039/C5SC02636A.
Guan, Xiaoyang, Chaffey, Patrick K., Zeng, Chen, Greene, Eric R., Chen, Liqun, Drake, Matthew R., Chen, Claire, Groobman, Ari, Resch, Michael G., Himmel, Michael E., Beckham, Gregg T., & Tan, Zhongping. Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module. United States. doi:10.1039/C5SC02636A.
Guan, Xiaoyang, Chaffey, Patrick K., Zeng, Chen, Greene, Eric R., Chen, Liqun, Drake, Matthew R., Chen, Claire, Groobman, Ari, Resch, Michael G., Himmel, Michael E., Beckham, Gregg T., and Tan, Zhongping. Mon . "Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module". United States. doi:10.1039/C5SC02636A. https://www.osti.gov/servlets/purl/1233680.
@article{osti_1233680,
title = {Molecular-Scale Features that Govern the Effects of O-Glycosylation on a Carbohydrate-Binding Module},
author = {Guan, Xiaoyang and Chaffey, Patrick K. and Zeng, Chen and Greene, Eric R. and Chen, Liqun and Drake, Matthew R. and Chen, Claire and Groobman, Ari and Resch, Michael G. and Himmel, Michael E. and Beckham, Gregg T. and Tan, Zhongping},
abstractNote = {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.},
doi = {10.1039/C5SC02636A},
journal = {Chemical Science},
issn = {2041-6520},
number = 12,
volume = 6,
place = {United States},
year = {2015},
month = {9}
}

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Cited by: 11 works
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