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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.7K
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...
2.7K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.6K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.6K
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.
Glycosylation occurs in...
6.4K
Protein Folding01:22

Protein Folding

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Overview
116.7K
Proteoglycans01:05

Proteoglycans

3.8K
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,...
3.8K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

3.4K
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.
3.4K

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関連する実験動画

Updated: May 12, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

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イオン機能群によるグリカン折り合いを制御する

Nishu Yadav1,2, Ana Poveda3, Yadiel Vázquez Mena1,4

  • 1Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam, Germany.

Journal of the American Chemical Society
|April 24, 2025
PubMed
まとめ
この要約は機械生成です。

研究者はイオン群を伴うグリカン配列を設計し その形状を制御した. このグリカン

さらに関連する動画

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

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関連する実験動画

Last Updated: May 12, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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科学分野:

  • 炭水化物の化学反応
  • 超分子化学
  • 材料科学

背景:

  • グリカン (炭水化物ベースのポリマー) は,形状の柔軟性を示す.
  • グライカンのイオン機能群は,その構造,動力,結合に影響する.
  • 自然界のシステムは 生物学的分子行動を制御するために イオン相互作用を利用します

研究 の 目的:

  • 制御可能な二次構造を持つ合成グリカン配列を設計する.
  • グライカンの形状を決定するイオン相互作用の役割を調査する.
  • 反応性のある材料としてのグリカンの可能性を探求する.

主な方法:

  • イオン置換剤をグリカン配列に戦略的に組み込む.
  • グライカンのヘアピン形状の設計
  • 外部刺激 (pH,酵素) を適用してグリカン構造を調節する.
  • 異なるプロトネーション状態でのグリカン集積の分析.

主要な成果:

  • エンジニアリングされたグリカン配列は ヘアピン形状を採用した.
  • 補完的なイオン群が 閉じたヘアピン構造を安定させました
  • イオン排斥は オープンなグリカン形状へのシフトを誘導しました
  • 外部刺激で動的に制御された ヘアピン開閉
  • 陽子化状態の変化がグリカン結合を誘発した.

結論:

  • イオン群は,グリカン二次構造を正確に制御する.
  • グライカンのダイナミックな構造の変化は,外部の刺激によって達成できます.
  • 反応性のあるグリカンベースの材料は,イオン相互作用と集積を使用して開発することができます.
  • この研究は,機能的なグリカンアーキテクチャの設計のための新しい戦略を提供します.