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

RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Redox Reactions01:27

Redox Reactions

Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...

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

Inducible rAAV producer cell lines yield vectors equivalent to transient transfection: a physicochemical and biological comparison.

Scientific reports·2026
Same author

Effect of surfactants on agitation-induced submicron and subvisible particles of therapeutic proteins.

Journal of pharmaceutical sciences·2026
Same author

Polymerization-Induced Functional Switching of Engineered Polyhydroxyalkanoate Synthase Directs Block Copolymerization.

Journal of the American Chemical Society·2026
Same author

Significance of Lipoprotein(a) in Coronary Artery Disease: A Comparative Study of Patients Undergoing Percutaneous Coronary Intervention and Healthy Individuals.

Circulation reports·2026
Same author

Manufacture of adeno-associated virus vectors by a novel human-derived cell line HAT and comprehensive evaluation of the vectors.

Molecular therapy. Advances·2026
Same author

Quantification of glyphosate and glufosinate in human blood using the aqueous layer recovered from QuEChERS extraction.

Analytical sciences : the international journal of the Japan Society for Analytical Chemistry·2026

相关实验视频

Updated: Jun 30, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

细胞染色体c的氧化还原功能和蛋白质稳定性之间的关系

Norifumi Terui1, Naoki Tachiiri, Hitomi Matsuo

  • 1Department of Chemistry, University of Tsukuba, Tsukuba 305-8571, Japan.

Journal of the American Chemical Society
|November 6, 2003
PubMed
概括
此摘要是机器生成的。

蛋白质的稳定性,特别是氧化形式,通过体贡献和Fe-methionine键调节,决定了细胞染色体的氧化还原潜力. 这影响了Pseudomonas aeruginosa和Hydrogenobacter thermophilus中的电子转移.

更多相关视频

Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein
06:10

Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein

Published on: June 18, 2020

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

相关实验视频

Last Updated: Jun 30, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein
06:10

Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein

Published on: June 18, 2020

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

科学领域:

  • 生物化学 生物化学
  • 生物物理学的生物物理.
  • 蛋白质科学 蛋白质科学

背景情况:

  • 细胞染色体c是关键的电子转移蛋白,参与各种生物过程.
  • 了解调节它们的氧化还原潜力的因素对于破译它们的功能至关重要.
  • 蛋白质的稳定性在蛋白质功能中起着重要作用,特别是在不同温度下.

研究的目的:

  • 为了研究中性Pseudomonas aeruginosa cytochrome c551和热性Hydrogenobacter thermophilus cytochrome c552.的蛋白质稳定性和氧化还原潜力之间的关系.
  • 阐明体因子对氧化还原潜力的贡献.
  • 确定氧化蛋白质形式的稳定性如何影响Fe-甲氨酸协调键和氧化还原功能.

主要方法:

  • 对纯化蛋白质及其突变物进行了电化学研究.
  • 核磁共振 (1H NMR) 光谱法用于评估蛋白质结构和动态.
  • 光学光谱学在广泛的温度范围内提供了对电子性质和氧化还原状态的洞察.

主要成果:

  • 稳定的蛋白质结构表现出较低的氧化还原潜力,主要是由对氧化还原反应的体贡献驱动的.
  • 氧化蛋白形式的稳定性与关键的Fe-甲氨酸协调键的稳定性直接相关.
  • 突变分析揭示了影响蛋白质稳定性和氧化还原性能的特定残留物.

结论:

  • 蛋白质稳定性是细胞染色体c中氧化还原潜力的关键决定因素,由性因子介导.
  • 由氧化蛋白形式的稳定性调节的Fe-氨酸协调键的稳定性,直接控制了氧化还原功能.
  • 这些发现为细胞染色体c的结构功能关系提供了基本的见解.