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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein Glycosylation01:25

Protein Glycosylation

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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Related Experiment Video

Updated: Jul 12, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

Cooperativity in glycan-protein interactions.

Rahul Raman1, Ram Sasisekharan

  • 1Department of Biological Engineering, Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.

Chemistry & Biology
|August 28, 2007
PubMed
Summary

Multivalency in glycan-protein interactions is crucial for achieving specific binding. The study models this using fibroblast growth factor 2 (FGF-2) and heparan sulfate glycosaminoglycans (HSGAGs).

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Glycan-protein interactions mediate numerous biological processes.
  • Specificity in these interactions is often challenging to achieve.
  • Heparan sulfate glycosaminoglycans (HSGAGs) are complex carbohydrates involved in cell signaling and adhesion.

Discussion:

  • The study by de Paz and colleagues utilizes fibroblast growth factor 2 (FGF-2) and HSGAGs as a model system.
  • This model highlights the role of multivalency in mediating specific glycan-protein binding.
  • Cooperative binding events are essential for enhancing interaction specificity.

Key Insights:

  • Multivalency, the simultaneous binding of multiple ligands to multiple receptors, significantly enhances binding affinity and specificity.
  • Cooperative interactions between FGF-2 and HSGAGs demonstrate how complex biological recognition can be achieved.
  • Understanding these principles is vital for deciphering cellular communication pathways.

Outlook:

  • Further investigation into multivalent interactions can lead to the development of novel therapeutics.
  • This research provides a foundation for designing synthetic molecules with tailored binding properties.
  • Exploring other glycan-protein systems will reveal the broader applicability of multivalency in biological recognition.