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関連する概念動画

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

4.6K
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
Regioselectivity of Electrophilic Additions-Peroxide Effect02:35

Regioselectivity of Electrophilic Additions-Peroxide Effect

11.0K
In the presence of organic peroxides, the addition of hydrogen bromide to an alkene yields the isomer that is not predicted by Markovnikov’s rule. For example, the addition of hydrogen bromide to 2-methylpropene in the presence of peroxides gives 1-bromo-2-methylpropane. This addition reaction proceeds via a free radical mechanism, which reverses the regioselectivity. The free radical reaction mechanism involves three stages: initiation, propagation, and termination.
11.0K
Regioselectivity and Stereochemistry of Hydroboration02:36

Regioselectivity and Stereochemistry of Hydroboration

9.5K
A significant aspect of hydroboration–oxidation is the regio- and stereochemical outcome of the reaction.
Hydroboration proceeds in a concerted fashion with the attack of borane on the π bond, giving a cyclic four-centered transition state. The –BH2 group is bonded to the less substituted carbon and –H to the more substituted carbon. The concerted nature requires the simultaneous addition of –H and –BH2 across the same face of the alkene giving syn stereochemistry.
9.5K

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関連する実験動画

Updated: Feb 14, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

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ネイティブタンパク質の化学および地域選択性ライシン改変

Maria J Matos1, Bruno L Oliveira1, Nuria Martínez-Sáez1

  • 1Department of Chemistry , University of Cambridge , Lensfield Road , Cambridge , U.K.

Journal of the American Chemical Society
|February 24, 2018
PubMed
まとめ

コンピュータで設計された反応剤は,ネイティブタンパク質の単一のリジン残基の正確な修正を可能にします. これは遺伝子工学なしで治療や生物学的研究のためのタンパク質結合を進める.

さらに関連する動画

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

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Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA
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Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA

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関連する実験動画

Last Updated: Feb 14, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

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Published on: April 4, 2018

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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA
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科学分野:

  • 生物結合化学
  • タンパク質工学
  • 化学生物学

背景:

  • タンパク質の改変は 治療的・機能的応用の拡大に不可欠です
  • 既存の方法はしばしば遺伝子改変を必要とするか,タンパク質の末端に限定される.
  • サイト選択的結合は,タンパク質化学における課題である.

研究 の 目的:

  • コンピュータで設計された反応剤を用いて,部位選択的なタンパク質改変のための新しい方法を開発する.
  • エンジニアリングなしでネイティブのタンパク質配列に単一のリジン残基の修正を達成する.
  • 機能的なタンパク質結合体を生成するためのこの方法の有用性を実証する.

主な方法:

  • サルフォニルアクリラート反応剤のコンピューター支援設計
  • リジン残基の固有反応性の差異を地域選択性のために利用する.
  • 生体適合条件 (37 °C,pH 8.0) で反応する.

主要な成果:

  • 治療用抗体トラストズマブを含む 5つの異なるタンパク質に単一のリジン残留物を成功裏に修正した.
  • ライシンpKaとローカルマイクロ環境に基づいてサイト選択性を達成し,計算で予測した.
  • サイステインなどの他の核愛体に比べて 化学的選択性を示した.
  • 細胞イメージングと診断のための機能的なタンパク質結合を作りました.

結論:

  • 開発された方法は,サイト選択的なタンパク質改変のためのシンプルで堅固な非遺伝的アプローチを提供します.
  • この技術は,多様な生物学的および治療的用途のための,明確に定義されたタンパク質結合物の作成を可能にします.
  • リージオセレクティブのライシン改変は,高度な応用のためのさらなる生物結合を容易にする.