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Histone Modification02:32

Histone Modification

16.3K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.3K
Histone Modification02:32

Histone Modification

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4.6K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.2K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.2K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

9.5K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
9.5K
Uncertainty in Measurement: Accuracy and Precision03:37

Uncertainty in Measurement: Accuracy and Precision

104.7K
Scientists typically make repeated measurements of a quantity to ensure the quality of their findings and to evaluate both the precision and the accuracy of their results. Measurements are said to be precise if they yield very similar results when repeated in the same manner. A measurement is considered accurate if it yields a result that is very close to the true or the accepted value. Precise values agree with each other; accurate values agree with a true value. 
104.7K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
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メチオニン特異的非可逆的バイオコンジュゲーション：精密タンパク質修飾の進歩

Shirui Wang1,2, Zhenguo Zhang1,2, Raymond Tio2

  • 1Department of Chemistry, School of Sciences, Great Bay University, Dongguan 523000, China.

Proceedings of the National Academy of Sciences of the United States of America
|February 10, 2026
PubMed
まとめ

活性化アリルブロミドを用いた新しいメチオニン選択的バイオコンジュゲーション法を開発した。このアプローチは、コンジュゲートの安定性を向上させ、化学生物学研究のための精密なタンパク質標識を可能にする。

キーワード:
活性化アリルブロミド後期修飾メチオニンバイオコンジュゲーションメチオニン特異性穏やかな条件

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科学分野:

  • 化学生物学
  • 有機化学
  • 生化学

背景:

  • メチオニンバイオコンジュゲーションはタンパク質修飾に不可欠である。
  • 既存のメソッドは安定性と非特異的反応性の課題に直面している。
  • 堅牢で選択的なメチオニン標識戦略の必要性が存在する。

研究 の 目的:

  • メチオニンを選択的な新規非可逆的バイオコンジュゲーション戦略を開発すること。
  • 従来のメソッドと比較して、コンジュゲート安定性を向上させ、非特異的反応を低減すること。
  • 共有結合性阻害剤設計およびタンパク質機能化における応用を実証すること。

主な方法:

  • 活性化アリルブロミドを穏やかな水性条件下で使用した。
  • この戦略を様々なペプチドおよびタンパク質に適用した。
  • コンジュゲートの安定性と特異性を評価した。

主要な成果:

  • ペプチドおよびタンパク質のメチオニン優先標識を達成した。
  • コンジュゲート安定性の向上を実証した。
  • 反応条件下での非特異的反応性を抑制した。
  • 共有結合性阻害剤設計およびタンパク質機能化の概念実証を示した。

結論:

  • 開発された戦略は、メチオニンバイオコンジュゲーションのための堅牢で選択的な方法を提供する。
  • この化学は、化学生物学におけるタンパク質修飾のための利用可能なツールを拡張する。
  • このアプローチは、穏やかな水性条件下でペプチドおよびタンパク質と適合する。