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Protein Glycosylation01:25

Protein Glycosylation

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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.
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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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.
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Oligosaccharide Assembly01:24

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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.
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Zygomycota, previously classified as a distinct fungal group, are primarily terrestrial, saprophytic molds that play a crucial role as decomposers. Recent phylogenetic studies have revealed that these fungi are now divided into two major clades — Mucoromycota, which includes many symbiotic species, and Zoopagomycota, which primarily consists of parasitic and pathogenic fungi. These groups exhibit distinct ecological roles and reproductive strategies while sharing key structural and...
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β-Glucans: Relationships between Modification, Conformation and Functional Activities.

Qiang Wang1, Xiaojing Sheng2, Aimin Shi3

  • 1Institute of Food Science and Technology, Chinese Academy of Agriculture Sciences, Beijing 100193, China. wangqiang06@caas.cn.

Molecules (Basel, Switzerland)
|February 18, 2017
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Summary

Beta-glucans, polysaccharides found in various organisms, exhibit diverse biological activities. Modifying their structure and conformation is key to optimizing these immune-enhancing and therapeutic effects.

Keywords:
conformation transformationfunctional activitiesmodificationβ-glucans

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Beta-glucans are polysaccharides with well-documented biological activities, including immune enhancement, antitumor, antibacterial, antiviral, and wound healing.
  • The specific conformation of beta-glucan significantly influences its bioactivity, leading to varied effects even among molecules with similar basic structures.
  • Modification of polysaccharides can alter their structure and intermolecular forces, inducing conformational changes in solution that directly impact bioactivity.

Purpose of the Study:

  • To review methods for modifying beta-glucan molecules.
  • To explore the relationship between beta-glucan conformation (flexible helix and helix form) and its bioactivities.
  • To summarize challenges and future directions in modifying beta-glucan conformation and function.

Main Methods:

  • Review of physical modification methods for beta-glucan.
  • Review of chemical modification methods for beta-glucan.
  • Review of biological modification methods for beta-glucan.

Main Results:

  • Different modification strategies (physical, chemical, biological) can alter beta-glucan structure and conformation.
  • Conformational changes, particularly in flexible helix and helix forms, are directly linked to variations in bioactivity.
  • Understanding these structure-activity relationships is crucial for harnessing beta-glucan's therapeutic potential.

Conclusions:

  • Modification of beta-glucan offers a pathway to tune its biological activities.
  • Further research into the precise control of beta-glucan conformation is needed to maximize its functional benefits.
  • Addressing scientific challenges in modification and conformational control will unlock future applications of beta-glucan.