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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.6K
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...
19.6K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Protein Complex Assembly02:41

Protein Complex Assembly

16.8K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.8K
Protein Complex Assembly02:41

Protein Complex Assembly

2.6K
2.6K
Histone Modification02:32

Histone Modification

16.2K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.2K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.1K
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...
7.1K

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

Identifying Antibiotic Effects of Investigational Drugs on Commensal Bacteria with Machine Learning.

ACS pharmacology & translational science·2026
Same author

Training and Communication Package for Acute Fever Case Management and Antibiotic Prescriptions: A Qualitative Exploration into Changing Behaviors of Healthcare Workers, Patients, and Caregivers in Chandigarh, India.

Indian journal of public health·2026
Same author

The Use of Deep Learning in RNA Therapeutic Development.

ACS nano·2026
Same author

Longitudinal Assessment of Psychological Distress and Coping Strategies in Animal Bite Victims Undergoing Rabies Post-Exposure Prophylaxis.

The American journal of tropical medicine and hygiene·2026
Same author

Plug-and-play assembly of biodegradable ionizable lipids for potent mRNA delivery and gene editing in vivo.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Profiling biological effects of microbiome metabolites via machine learning.

iScience·2026

相关实验视频

Updated: Feb 7, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K

合成内在无序蛋白质的基因编码的固醇修饰驱动其自我组装成不同的形态.

Sarah Yeon-Kyoung Kim1, Taranpreet Kaur2, Yulia Shmidov2

  • 1Department of Chemistry and Biochemistry, Washington and Lee University, Lexington, Virginia, USA.

Small (Weinheim an der Bergstrasse, Germany)
|February 6, 2026
PubMed
概括

研究人员通过将固醇连接到多来创造了新的脂蛋白生物材料 (STaMPs). 这些STaMP显示自组装和基于固醇特性改变的热行为,扩大生物材料的可能性.

关键词:
类似于弹性质的多类.脂肪化 脂化 脂化翻译后的修改.蛋白质工程工程 蛋白质工程自动组装的自动组装机

更多相关视频

Rapid, Scalable Assembly and Loading of Bioactive Proteins and Immunostimulants into Diverse Synthetic Nanocarriers Via Flash Nanoprecipitation
06:57

Rapid, Scalable Assembly and Loading of Bioactive Proteins and Immunostimulants into Diverse Synthetic Nanocarriers Via Flash Nanoprecipitation

Published on: August 11, 2018

8.4K
Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity
12:31

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Published on: May 1, 2018

14.8K

相关实验视频

Last Updated: Feb 7, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Rapid, Scalable Assembly and Loading of Bioactive Proteins and Immunostimulants into Diverse Synthetic Nanocarriers Via Flash Nanoprecipitation
06:57

Rapid, Scalable Assembly and Loading of Bioactive Proteins and Immunostimulants into Diverse Synthetic Nanocarriers Via Flash Nanoprecipitation

Published on: August 11, 2018

8.4K
Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity
12:31

Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

Published on: May 1, 2018

14.8K

科学领域:

  • 生物材料科学 生物材料科学
  • 蛋白质工程是指蛋白质工程.
  • 聚合物化学 聚合物化学

背景情况:

  • 翻译后修改 (PTMs) 自然地将蛋白质功能扩展到20个氨基酸之外.
  • PTMs改变了蛋白质的结构和功能,为新的生物材料设计提供了途径.
  • 脂质-蛋白质结合物受到自然系统的启发,以获得先进的材料特性.

研究的目的:

  • 合成和表征新的固醇结合多 (STaMPs).
  • 为了研究STaMPs的自我组装行为,以应对不同的固醇疏水性.
  • 探索醇结合如何影响弹性类多 (ELPs) 的热特性.

主要方法:

  • 通过将特定的固醇 (coprostanol, epicoprostanol, androstanol, galeterone, dehydroepiandrosterone) 与ELP结合,合成五种STaMP变体.
  • 使用技术来评估解决方案行为的STaMP自组装的特征.
  • 评估固醇疏水性对ELP较低临界溶液温度 (LCST) 行为的影响.

主要成果:

  • STaMPs表现出固醇依赖的自我组装,根据固醇的疏水性形成随机的线圈或球状小粒.
  • 附加的固醇的疏水性可预测地调节了ELP的LCST行为.
  • 成功创建了具有可调节性质的混合脂蛋白生物材料.

结论:

  • 固醇结合为控制多的自我组装和热反应提供了一种多功能策略.
  • STaMPs代表了一种新的生物材料类别,在药物输送,组织工程和纳米技术方面具有潜在的应用.
  • 这些发现突显了脂质和蛋白质成分在设计功能生物材料中的协同作用.