Protein Native-State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns
Open accessAbstract
Protein reverse turns that interact with a phenlyalanine group allow stable introduction of glycan groups at asparagine residues.
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The exact context of the sequon can dictate the outcome of initial protein folding.
“Even at the level of initial protein folding the exact context of the sequon can dictate the outcome.”
From Biological roles of glycans (2017) · cites this paper as [497]
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“For example, experimentally placing a phenylalanine residue two or three positions before a glycosylated asparagine in distinct reverse turns facilitates stabilizing interactions between the aromatic side chain and the first GlcNAc residue of the glycan, while increasing glycosylation efficiency (497).”
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- Authors
- Culyba, E. K., Price, J. L., Hanson, S. R., Dhar, A., Wong, C.-H., Gruebele, M., Powers, E. T., & Kelly, J. W.
- Affiliations
- Scripps Research Institute (US)
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Culyba, Elizabeth K.
- Price, Joshua L.
- Powers, Evan T.
- Kelly, Jeffery W.
- ORCID
- Venue
- Science
- Published
- 2011-02-04
- Volume
- 331
- Issue
- 6017
- Pages
- 571-575
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3099596
- OpenAlex
- W2088816092
- Cited by
- 171
- References
- 29
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 4 · 2023: 2 · 2022: 9 · 2021: 12 · 2020: 5 · 2019: 7 · 2018: 16 · 2017: 15 · 2016: 16 · 2015: 15 · 2014: 18 · 2013: 14 · 2012: 17
- FWCI
- 7.91
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (F32 GM086039, AI072155)
- National Science Foundation (MCB 1019958)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- N-glycosylation, protein stability, beta-turn, aromatic side chains, phenylalanine, asparagine-linked glycosylation, N-acetylglucosamine, protein folding, secretory pathway, glycosylation efficiency
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Acylphosphatase, Acetylglucosamine, Amino Acid Sequence, Animals, Asparagine, Glycosylation, Humans, Models, Molecular, Phenylalanine, Polysaccharides, Protein Conformation, Thermodynamics, Protein Engineering, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Protein Folding, Acid Anhydride Hydrolases, CD2 Antigens, Peptidylprolyl Isomerase, Mutant Proteins, Rats, Protein Stability
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