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Related Concept Videos

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...
Proteoglycans01:05

Proteoglycans

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,...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Exploring the C-H...O interactions in glycoproteins.

Sudha Anand1, Anand Anbarasu, Rao Sethumadhavan

  • 1Bioinformatics & Computational Biology Division, School of Biotechnology, Chemical & Biomedical Engineering, Vellore Institute of Technology, Vellore 632014, India.

Applied Biochemistry and Biotechnology
|January 22, 2009
PubMed
Summary

Carbon-hydrogen bonded to oxygen (CH...O) interactions are crucial for stabilizing glycoproteins. These interactions, particularly long-range ones, significantly contribute to the overall structural integrity of these vital biomolecules.

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

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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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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

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Glycoproteins are essential biomolecules involved in numerous cellular processes.
  • Understanding the forces that stabilize glycoprotein structure is key to deciphering their function.
  • Carbon-hydrogen bonded to oxygen (CH...O) interactions are increasingly recognized as significant non-covalent forces in protein stabilization.

Purpose of the Study:

  • To investigate the role and influence of CH...O interactions in glycoprotein structural stability.
  • To analyze the contribution of CH...O interactions in the context of other environmental factors affecting glycoproteins.
  • To identify specific residues and patterns of CH...O interactions involved in stabilization.

Main Methods:

  • Analysis of existing glycoprotein structural data.
  • Identification and characterization of CH...O interactions within glycoprotein structures.
  • Comparison of interacting residues and their conservation across different glycoproteins.
  • Assessment of the spatial distribution (short-range vs. long-range) of CH...O contacts.

Main Results:

  • CH...O interactions are a significant factor in glycoprotein stabilization, acting as genuine hydrogen bonds.
  • Main chain-main chain interactions involving CH...O bonds are predominant.
  • Proline residues frequently utilize CH...O interactions to stabilize secondary structures like strands.
  • A majority of residues involved in CH...O interactions are conserved and possess stabilization centers.
  • Long-range CH...O contacts are prevalent, suggesting a role in global conformational stability.

Conclusions:

  • CH...O interactions are vital for maintaining the global conformational stability of glycoproteins.
  • The findings provide valuable insights for future studies on glycoprotein structural stability.
  • Understanding these interactions can aid in protein engineering and drug design targeting glycoproteins.