Glycoprotein Folding
Glycoprotein Folding - Related Videos
08:58
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Cited by 5 •
2018
We present approaches for the biophysical and structural characterization of glycoproteins with the immunoglobulin fold by biolayer interferometry, isothermal titration calorimetry, and X-ray crystallography.
05:42
Using a Sandwich ELISA to Determine the Immunogenic Glycoprotein Content in a Vaccine
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2025
This video showcases an indirect enzyme-linked immunosorbent assay or ELISA sandwich immunocapture assay designed to assess immunogenic glycoprotein levels in vaccines. The assay plate, containing glycoprotein-specific antibodies, is incubated with serially diluted vaccine samples, including reference and test vaccines, followed by immunoassay to quantify glycoprotein content in the test vaccine.
03:00
Molecular Chaperones and Protein Folding
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2020
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein. The...
01:49
Protein Folding
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2020
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation which is critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.Protein Structure Is Critical to Its Biological FunctionProteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:49
Protein Folding
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2026
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation which is critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.Protein Structure Is Critical to Its Biological FunctionProteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
FAQs
N-linked glycans contribute to maturation by providing structural features recognized during the folding process. Their presence works alongside disulfide-bond formation and ER chaperones, including calnexin and calreticulin, to guide newly synthesized glycoproteins toward suitable conformations. This coordination helps determine whether a molecule can continue through maturation or must remain in a quality-control cycle.
Calnexin and calreticulin act as chaperones that assist glycoproteins while they mature in the endoplasmic reticulum. They help coordinate folding with the processing of N-linked glycans, giving incompletely folded molecules opportunities to reach a functional structure. Their activity supports cellular quality control by separating molecules that can mature from those that require additional folding or degradation.
A molecule that fails to fold correctly does not simply proceed through the cell unchecked. Endoplasmic-reticulum quality-control mechanisms can retain it for additional folding cycles or direct it toward degradation. This response limits the accumulation of unstable proteins and connects glycoprotein folding with proteostasis, the cellular maintenance of a balanced and functional protein population.
A typical analysis follows the polypeptide as it enters the endoplasmic reticulum, then examines N-linked glycan handling, disulfide-bond formation, and interactions with calnexin or calreticulin. Researchers also assess whether the molecule completes maturation, remains in quality-control cycles, or undergoes degradation. Tracking these stages reveals where folding succeeds or becomes defective.
It becomes especially relevant when researchers need proteins that retain appropriate activity, stability, and manufacturability. Folding mechanisms help explain how therapeutic proteins and vaccine-related glycoproteins mature, while glycoengineering strategies can be designed to improve desirable production or functional properties. Understanding the underlying cellular process therefore supports more deliberate protein-design and manufacturing approaches.
Folding defects provide a way to connect molecular processing with disease mechanisms. If glycoproteins remain misfolded, quality-control cycles and degradation can alter the amount of functional protein available to the cell. Studying these outcomes helps researchers investigate disrupted proteostasis and identify how errors in maturation may affect secretion, membrane protein production, or cell-recognition functions.