ArticleProceedings of the National Academy of Sciences of the United States of America2010
Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 86 citations in OpenAlex.
- Site-specific N-glycoproteomics reveals alteration of N-glycan structures and heterogeneity to enhance thermally induced gelation characteristics of egg white proteins.Food chemistry: X · 2026Article
- Lubricin's Mucin Domain Has Strong Polyproline Type II Helical Character.Computational and structural biotechnology journal · 2026Article
- Theoretical Study of the Influence of K20N Glycosylation on the Dynamic Behavior of Im7 Protein.Molecules (Basel, Switzerland) · 2025Article
- Effect of glycosylation on protein folding: From biological roles to chemical protein synthesis.iScience · 2025Review
- Protein Glycosylation Patterns Shaped By the IRE1-XBP1s Arm of the Unfolded Protein Response.Israel journal of chemistry · 2024Article
- The origin of mutational epistasis.European biophysics journal : EBJ · 2024Article
- Solution Behavior of Glyco-Copoly(l-Glutamic Acid)s in Dilute Saline Solution.Biomacromolecules · 2024Article
- Uncloaking the viral glycocalyx: How do viruses exploit glycoimmune checkpoints?Advances in virus research · 2024Review
- Protein folding rate evolution upon mutations.Biophysical reviews · 2023Review
- Glycosylation increases active site rigidity leading to improved enzyme stability and turnover.The FEBS journal · 2023Article
- Expression of a Salt-Tolerant Pseudolysin in Yeast for Efficient Protein Hydrolysis under High-Salt Conditions.Biomolecules · 2022Article
- Thirty years of molecular dynamics simulations on posttranslational modifications of proteins.Physical chemistry chemical physics : PCCP · 2022Review
- Selective reaction monitoring approach using structure-defined synthetic glycopeptides for validating glycopeptide biomarkers pre-determined by bottom-up glycoproteomics.RSC advances · 2022Article
- Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022Article
- Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Stereoelectronic effects in stabilizing protein-N-glycan interactions revealed by experiment and machine learning.Nature chemistry · 2021Article
- Article
- Structure and Dynamics of N-Glycosylated Human Ribonuclease 1.Biochemistry · 2020Article
- Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019Review
- Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
N-linked glycosylation modulates protein folding and stability through a variety of mechanisms. As such there is considerable interest in the development of general rules to predict the structural consequences of site-specific glycosylation and to understand how these effects can be exploited in the design and development of modified proteins with advantageous properties. In this study, expressed protein ligation is used to create site-specifically glycosylated variants of the bacterial immunity protein Im7 modified with the chitobiose disaccharide (GlcNAc-GlcNAc). Glycans were introduced at seven solvent exposed sites within the Im7 sequence and the kinetic and thermodynamic consequences of N-linked glycosylation analyzed. The ΔΔG° values for glycan incorporation were found to range from +5.2 to -3.8 kJ·mol(-1). In several cases, glycosylation influences folding by modulating the local conformational preferences of the glycosylated sequence. These locally mediated effects are most prominent in the center of α-helices where glycosylation negatively effects folding and in compact turn motifs between segments of ordered secondary structure where glycosylation promotes folding and enhances the overall stability of the native protein. The studies also provide insight into why glycosylation is commonly identified at the transition between different types of secondary structure and when glycosylation may be used to elaborate protein structure to protect disordered sequences from proteolysis or immune system recognition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.