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

9.5K
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...
9.5K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.6K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.6K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.4K
4.4K
Protein and Protein Structure02:15

Protein and Protein Structure

87.2K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.2K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.1K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.1K
What are Proteins?01:55

What are Proteins?

238.2K
Overview
238.2K

You might also read

Related Articles

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

Sort by
Same author

Distinct properties of Halobacterium salinarum Agl32, an archaeal D-glucuronyl C5-epimerase involved in N-glycosylation.

Glycobiology·2026
Same author

Only in Halobacterium salinarum: Sugar modifications unique to an archaeal N-linked glycan.

Carbohydrate research·2026
Same author

Identification of the D-glucuronyl C5-epimerase that introduces iduronic acid into N-linked glycans decorating archaeal glycoproteins.

Communications biology·2025
Same author

Two different sulfotransferases modify sugars of the N-linked tetrasaccharide decorating <i>Halobacterium salinarum</i> glycoproteins.

mBio·2025
Same author

N-glycosylation in Archaea - Expanding the process, components and roles of a universal post-translational modification.

BBA advances·2024
Same author

Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility.

Nature communications·2024
Same journal

Hunting ecology predicts eye arrangements in the modular visual system of spiders.

Current biology : CB·2026
Same journal

Sub-second fluctuations between top-down and bottom-up modes distinguish diverse human brain states.

Current biology : CB·2026
Same journal

Queen bees offload pesticide burden to eggs when social buffering is overwhelmed.

Current biology : CB·2026
Same journal

Pitch selectivity in ferret auditory cortex.

Current biology : CB·2026
Same journal

A cell size-dependent competition between geometry and polarity governs nuclear and spindle positioning in early embryos.

Current biology : CB·2026
Same journal

Trophic cascades drive sustainability in the agricultural heritage rice-fish coculture system.

Current biology : CB·2026
See all related articles

Related Experiment Video

Updated: Jan 26, 2026

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

7.1K

Protein glycosylation.

Jerry Eichler1

  • 1Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.

Current Biology : CB
|April 3, 2019
PubMed
Summary
This summary is machine-generated.

This study explores the wide variety of protein glycosylations, which are crucial modifications that control how proteins function within cells.

More Related Videos

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
11:27

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

9.3K
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
20:23

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

Published on: October 1, 2009

16.5K

Related Experiment Videos

Last Updated: Jan 26, 2026

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

7.1K
Analysis of SCAP N-glycosylation and Trafficking in Human Cells
11:27

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

9.3K
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
20:23

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

Published on: October 1, 2009

16.5K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein glycosylation is a vital post-translational modification.
  • Diverse glycans are attached to proteins, influencing their biological roles.

Purpose of the Study:

  • To introduce the broad spectrum of protein glycosylation types.
  • To elucidate the regulatory functions of glycosylation in protein activity.

Main Methods:

  • Review of existing literature on protein glycosylation.
  • Analysis of the impact of glycosylation on protein structure and function.

Main Results:

  • Detailed overview of different protein glycosylation patterns.
  • Examples illustrating how glycosylation modulates protein interactions and signaling pathways.

Conclusions:

  • Protein glycosylation is a highly diverse and essential regulatory mechanism.
  • Understanding glycosylation is key to comprehending protein function and cellular processes.