Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Interfacial Characteristics of Ti/Steel Joints Welded by Resistance Spot Welding with Bi-Interlayer of Nb-Ni.

Materials (Basel, Switzerland)·2026
Same author

Structural Pockets and Interacting RNA-Associated Ligands (SPIRAL): A DSSR-enabled Meta-Analysis of RNA-Small Molecule Recognition.

bioRxiv : the preprint server for biology·2026
Same author

Cohort profile: PeRiOperative sTress risk assEssment and Clinical decision cohorT (PROTECT), a multi-center observational study based on real-world data.

BMC geriatrics·2026
Same author

Tracking Seamless All-Hour PM<sub>2.5</sub> in China Using a Gridded Surface Visibility-Based Transformer Model.

Environmental science & technology·2026
Same author

NMR-Based Fragment Screening for RNA-Targeted Drug Discovery.

Molecules (Basel, Switzerland)·2026
Same author

AI for atmosphere-ocean sciences: advancements, challenges and ways forward.

National science review·2026

関連する実験動画

Updated: May 18, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

マクロ分子混雑とタンパク質の安定性

Yaqiang Wang1, Mohona Sarkar, Austin E Smith

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Journal of the American Chemical Society
|September 8, 2012
PubMed
まとめ
この要約は機械生成です。

細胞化学は,タンパク質の混雑によって影響を受けます. ハードコアの反発だけでなく,化学相互作用も,混雑した環境におけるタンパク質の安定性に重大な影響を及ぼします.

さらに関連する動画

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
09:14

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding

Published on: August 22, 2016

関連する実験動画

Last Updated: May 18, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
09:14

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding

Published on: August 22, 2016

科学分野:

  • バイオケミストリー バイオケミストリー
  • 化学物理 化学物理
  • 分子生物学は分子生物学である.

背景:

  • 細胞環境は混雑し,タンパク質の安定性と機能に影響を及ぼします.
  • タンパク質の安定性は,排除された体積 (ハードコア) と化学相互作用によって影響されます.
  • 以前の研究では,混雑効果の主な原動力として,ハードコアの反発を強調することが多かった.

研究 の 目的:

  • 混雑した環境下におけるタンパク質の安定性に対するハードコアの排斥と化学相互作用の両方の貢献を調査する.
  • タンパク質の安定性に対する混雑効果のエントロピーとエンタルピー成分を定量化するために.
  • 細胞環境におけるタンパク質の行動の背後にあるメカニズムを解明する.

主な方法:

  • 核磁共振 (NMR) で検出されたアミドによる陽子交換を用いて,温度依存度を測定した.
  • エントロピーとエンタルピックの貢献を抽出するために,温度に依存するデータを分析した.
  • 混雑効果を評価するためのモデルタンパク質としてユビキチンに焦点を当てた.

主要な成果:

  • 化学相互作用は,混雑した環境におけるタンパク質の安定性に大きく貢献します.
  • 化学相互作用の影響は,しばしばハードコアの反発の影響を上回ります.
  • タンパク質の安定性に対する群集効果は,エントロピックとエンタルピック要因の複雑な相互作用である.

結論:

  • 化学相互作用とハードコア反発の両方が,混雑した生物系におけるタンパク質の安定性を理解するために重要である.
  • この発見は,以前の混雑研究におけるハードコア反発への優位な焦点を異視しています.
  • この研究は,細胞内で観察されたタンパク質の安定性と動態についてより包括的な説明を提供します.