Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

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...

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
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

相关实验视频

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

基堆叠控制了AT DNA中的兴奋状态动态.

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
概括

DNA光稳定性是防止紫外线突变的关键. 这项研究表明,基堆叠,而不是基配对,控制了DNA中的兴奋电子状态,形成保护遗传密码的极致体.

科学领域:

  • 摄影化学的使用.
  • 分子生物学分子生物学
  • 生物物理学的生物物理.

背景情况:

  • 太阳紫外线 (UV) 辐射诱导DNA中的兴奋电子状态,可能导致突变.
  • 酶性修复机制可以抵消DNA光损伤,但在能源上很昂贵.
  • DNA的内在光稳定性对生命至关重要,但在双螺旋中能量消散的机制尚未完全理解.

研究的目的:

  • 为了研究基堆叠与基配对在DNA电子能量消散中的作用.
  • 阐明控制DNA光稳定性的机制,特别是在腺因-胺序列中.

主要方法:

  • 研究了由腺因 (A) 和胆氨酸 (T) 基组成的单链和双链寡核酸.
  • 研究激发的单点电子状态及其衰变路径.
  • 分析了线内极致体状态的形成和寿命.

主要成果:

  • 垂直的基堆叠,而不是基配对,决定了DNA寡核酸中的兴奋电子状态的命运.
  • 链内排外体状态,寿命为50-150皮秒,当腺因基与自身或胺堆叠时,很容易形成.
  • 排外体形成将激发能量限制在B型双螺旋中的单一链中.

结论:

更多相关视频

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

相关实验视频

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

  • 基堆是DNA激发状态衰变的主要决定因素,促进非辐射能量消散.
  • 在DNA中形成的突变分子通过限制能量转移到一个链而保护遗传物质,允许补充链作为修复模板.