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

Protein Folding01:22

Protein Folding

118.7K
Overview
118.7K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.1K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.1K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

3.2K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.6K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.6K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.4K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.4K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.0K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.0K

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

hexABC seeking the physical code of DNA.

Nature communications·2026
Same author

Modeling Xanthophyll Excited States via Cost-Effective Quantum Chemistry methods and Property-Based Diabatization.

Journal of chemical theory and computation·2026
Same author

Why Do PETases Struggle with Crystalline PET? Catalytic Ensemble Sampling Reveals Molecular Bottlenecks.

The journal of physical chemistry letters·2026
Same author

Making excited state MD faster: Extrapolation of transition densities for TD-DFT calculations.

The Journal of chemical physics·2026
Same author

Vibronic Reorganization Suppresses Salinixanthin-to-Retinal Energy Transfer in the Freshwater Kin4B8 Xanthorhodopsin.

The journal of physical chemistry letters·2026
Same author

An Efficient PCM Scheme for ESA Oscillator Strengths within the Unrelaxed TD-DFT Approximation.

Journal of chemical theory and computation·2026

関連する実験動画

Updated: Aug 11, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.3K

pHに依存するキャピングの相互作用は,i-モチーフの大規模な構造的移行を誘導する

Israel Serrano-Chacón1,2, Bartomeu Mir1,3, Lorenzo Cupellini2

  • 1Instituto de Química Física "Rocasolano", CSIC, Serrano 119, 28006Madrid, Spain.

Journal of the American Chemical Society
|February 6, 2023
PubMed
まとめ

この研究はDNAオリゴヌクレオチドを

さらに関連する動画

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.5K
Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening
14:04

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Published on: January 16, 2021

4.8K

関連する実験動画

Last Updated: Aug 11, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.3K
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

15.5K
Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening
14:04

Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

Published on: January 16, 2021

4.8K

科学分野:

  • 生物化学
  • 分子生物学
  • 構造生物学

背景:

  • DNAはイモチーフのような 非正規の構造を形成します
  • DNAイモチーフの安定性と構造はpHと温度に敏感です.
  • DNAの構造的な可塑性を理解することは 分子生物学にとって極めて重要です

研究 の 目的:

  • 2つの異なるi-モチーフ構造を形成できるDNAオリゴヌクレオチドを調査する.
  • これらのi-モチーフのpHと温度依存の安定性を明らかにする.
  • i-モチーフ構造の間のコンフォメーションの切り替えを駆動する分子メカニズムを探求する.

主な方法:

  • DNA構造の生体物理的特徴
  • pHと温度安定性試験
  • 形状の変化を分析する分子動力学シミュレーション

主要な成果:

  • DNAオリゴヌクレオチドは,pHに依存する2つのiモチーフ構造を形成する.
  • 中性pHはC:C+塩基対とG:C:G:Cテトラッドを持つ構造を好みます.
  • 酸性pH (pH5) は,C:C+塩基対とG:T:G:Tテトラッドを持つ長方形のiモチーフを誘導する.
  • 細胞細胞のプロトネーション状態は 構造間の移行を促します
  • コンフォーマーションスイッチは,i-モチーフの展開なしに発生します.

結論:

  • 2つの異なるi-モチーフDNA構造の間で初めて観察された形状の切り替えを示しています.
  • iモチーフDNAモチーフのpH依存性の有意性を強調しています.
  • i-モチーフの構造は 完全に展開することなく ダイナミックな移行を遂げることができます