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

Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in 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

Photodynamics of amino acids under UV excitation: Extraterrestrial amino acids.

The Journal of chemical physics·2026
Same author

Development of a Nucleoside Photosensitizer Efficiently Activated by One- or Two-Photon Absorption in the Optical Therapeutic Window.

Journal of the American Chemical Society·2026
Same author

Common Photoproperties of Eumelanin and Natural Organic Matter Emerge from Ensembles of Few-Layered Nanostructures.

ACS central science·2026
Same author

Double Thionation of 4-Dimethylaminophthalimide Leads to the Development of a Highly Effective Photosensitizer.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Impacts of Fluorination at the Ortho-Position of Carboxy Groups on Tetrakis(biphenyl)ethene-Based Hydrogen-Bonded Framework.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Modulating the cytotoxic activity of Titanocene complexes through aliphatic chain modification to optimize albumin affinity.

Bioorganic chemistry·2026

関連する実験動画

Updated: Jun 17, 2026

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
11:01

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: April 1, 2010

塩基堆積は,AT DNAの興奮状態のダイナミクスを制御する.

Carlos E Crespo-Hernández1, Boiko Cohen, Bern Kohler

  • 1Department of Chemistry, The Ohio State University, 100 W. 18th Avenue, Columbus, Ohio 43210, USA.

Nature
|August 27, 2005
PubMed
まとめ

紫外線からの突然変異を防ぐには,DNAの光安定性が重要です. この研究は,塩基配列ではなく,塩基堆積がDNAの興奮電子状態を制御し,遺伝コードを保護するエクシマーを形成することを明らかにしています.

科学分野:

  • フォトケミストリー フォトケミストリー
  • 分子生物学は分子生物学である.
  • バイオフィジックス 生物物理学

背景:

  • 太陽の紫外線 (UV) 放射線はDNAに電子状態を誘発し,潜在的に変異を引き起こす可能性があります.
  • 酵素修復メカニズムはDNAの光傷害に対抗しますが,エネルギー的に高価です.
  • DNAの固有の光安定性は生命にとって不可欠ですが,二重ヘリクスのエネルギー分散のメカニズムは完全に理解されていません.

研究 の 目的:

  • DNAにおける電子エネルギーの消散における塩基配列対塩基配列の役割を調査する.
  • DNAの光安定性を支配するメカニズム,特にアデニン-チミン配列の解明.

主な方法:

  • アデニン (A) 塩基とチミン (T) 塩基から成る単一および二重鎖のオリゴヌクレオチドを研究した.
  • 刺激されたシングレット電子状態とその崩壊経路を研究した.
  • イントラストランドエクシマー状態の形成と寿命を分析した.

主要な成果:

  • ベースペアリングではなく,垂直ベーススタッキングは,DNAオリゴヌクレオチドの興奮電子状態の運命を決定する.
  • 50-150ピコ秒の寿命を持つイントラストランドエクシマー状態は,アデニン塩基が自分自身またはチミンと積み重なると容易に形成されます.

さらに関連する動画

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
09:17

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

関連する実験動画

Last Updated: Jun 17, 2026

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
11:01

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: April 1, 2010

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
09:17

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

  • エクシマーの形成は,刺激エネルギーをB型ダブルヘリックス内の単一鎖に制限する.

    • 結論:

    • 塩基の積み重ねは,DNAの興奮状態の崩壊の主な決定因子であり,非放射性エネルギーの分散を促進します.
    • DNAにおけるエクシマーの形成は,一本の鎖にエネルギー転送を制限することによって,遺伝物質を保護し,補完的な鎖が修復のためのテンプレートとして機能することを可能にします.