Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

8.3K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
8.3K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.6K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
2.6K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

4.3K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
4.3K
Proteoglycans01:05

Proteoglycans

4.0K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.0K
Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

979
Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
979
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.6K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

1-Year Real-World Outcomes With the Amulet Occluder From the EMERGE LAA Postapproval Study.

JACC. Cardiovascular interventions·2026
Same author

Incidence, Predictors, Management, and Clinical Impact of Major Bleeding Following Left Atrial Appendage Occlusion: The Amulet IDE Randomized Clinical Trial.

JAMA cardiology·2026
Same author

Corrigendum to '2025 SCAI/HRS Clinical Practice Guidelines on Transcatheter Left Atrial Appendage Occlusion': [Journal of the Society for Cardiovascular Angiography & Interventions. Volume 4, Issue 9 (2025) 103783].

Journal of the Society for Cardiovascular Angiography & Interventions·2026
Same author

Early Outcomes With a Next-Generation Dual-Seal Left Atrial Appendage Occluder: Results From the VERITAS Study.

JACC. Clinical electrophysiology·2026
Same author

Genetic evaluation of early-onset atrial fibrillation: impact on patient management.

European heart journal·2025
Same author

Comparative Outcomes of Intracardiac vs Transesophageal Echocardiographic Guidance for Left Atrial Appendage Occlusion: Insights From EMERGE LAA Postapproval Study.

JACC. Cardiovascular interventions·2025
Same journal

From Cation Solvation to Anion Coordination: Lewis-Acidic Boranes Enable Halide Salt Electrolytes.

The journal of physical chemistry. B·2026
Same journal

In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.

The journal of physical chemistry. B·2026
Same journal

Metastructure Analysis of Self-Assembled Nanocubes with Different Equatorial Methyl Groups Based on Molecular Dynamics Simulations.

The journal of physical chemistry. B·2026
Same journal

A Cocoordinated <sup>1</sup>H Internal Reference Quantifies Proton-Exchange Bias in Coordinated-Water Diffusion.

The journal of physical chemistry. B·2026
Same journal

Unveiling Electrolyte-Dependent Coordination Site Dynamics for Redox Mediator Design in Lithium-O<sub>2</sub> Batteries: Exchange vs Rearrangement.

The journal of physical chemistry. B·2026
Same journal

The Role of Functional Groups in Substituted Benzoic Acids Used as Dopants in Liquid Crystal Mixtures on the Nematic-Isotropic Transitions.

The journal of physical chemistry. B·2026
See all related articles

Related Experiment Video

Updated: Apr 24, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

36.9K

Deciphering the glycosylation code.

Christopher R Ellis1, William G Noid

  • 1Department of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.

The Journal of Physical Chemistry. B
|September 5, 2014
PubMed
Summary
This summary is machine-generated.

Glycosylation impacts protein structure, but the "glycosylation code" is unknown. Molecular dynamics simulations reveal that nearby amino acids, not aromatic interactions, significantly influence glycosylation effects on protein folding and stability.

More Related Videos

Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

10.1K
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.0K

Related Experiment Videos

Last Updated: Apr 24, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

36.9K
Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

10.1K
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.0K

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Chemistry

Background:

  • Asparagine-linked carbohydrates are crucial for glycoprotein folding, stability, and structure.
  • The precise relationship between glycosylation and protein sequence, known as the "glycosylation code," remains largely undeciphered.

Purpose of the Study:

  • To investigate the impact of glycosylation on peptide structure and stability using molecular dynamics simulations.
  • To elucidate the biophysical principles governing the "glycosylation code."

Main Methods:

  • Atomically detailed replica exchange molecular dynamics simulations in explicit solvent.
  • Systematic investigation of glycosylation effects on peptides with the sequon Pro-Asn-Gly/Ala-Thr-Trp/Ala.
  • Comparison of simulated ensembles with known structures of full-length glycoproteins.

Main Results:

  • Glycosylation's impact is sensitive to steric crowding by the side chain following the glycosylation site.
  • Aromatic stacking interactions with tryptophan residues have a lesser effect on glycosylation outcomes.
  • Simulated data align with known glycoprotein structures, indicating consistency in intraprotein and protein-glycan interactions.
  • Left-handed conformations are significant for compact beta-hairpins at glycosylation sites.

Conclusions:

  • Glycosylation effects are influenced by local steric factors rather than long-range aromatic interactions.
  • Simulations provide insights into the "glycosylation code" and its underlying biophysical principles.
  • Consistent interactions between proteins and glycans are observed in both simulated and natural glycoproteins.