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相关概念视频

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.
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones01:24

Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones

Acetals are formed by reacting two equivalents of alcohol with carbonyl compounds like aldehydes or ketones. Acetals are unaffected by bases, nucleophiles, oxidizing agents, and reducing agents. They serve as protecting groups for aldehydes and ketones. Acetals can be easily formed and also easily removed via mild acid hydrolysis.
In the presence of multiple functional groups, when selective reduction of one group over the other is desired, groups like aldehydes and ketones that form acetals...

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相关实验视频

Updated: May 9, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

可调节的铁作为无痕可逆蛋白质PEGylation的"减少"响应功能.

Jianwei Chen1, Mingkun Zhao, Fude Feng

  • 1Department of Pharmacology, Dan L. Duncan Cancer Center, and Cardiovascular Research Institute, Baylor College of Medicine, Houston, Texas 77030, USA.

Journal of the American Chemical Society
|July 16, 2013
PubMed
概括

铁化学提供了一种新的,可调节的替代方案,用于减少响应药物递送的二硫化物键. 这种对硫醇有反应的系统更容易合成,并且比传统方法提供了更广泛的动力控制.

更多相关视频

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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Published on: October 4, 2017

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: May 9, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

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:

  • 化学生物学 化学生物学
  • 药物输送系统 药物输送系统
  • 材料科学 材料科学 材料科学

背景情况:

  • 双硫化物键是当前药物输送技术中使用的首要减少反应触发器.
  • 现有的基于二硫化物的系统在合成可访问性和动态可调性方面存在局限性.

研究的目的:

  • 介绍和描述作为一种新的醇反应化学物质,用于先进的药物输送应用.
  • 通过修改它们的硬质环境来探索可调节的铁的反应性.
  • 开发一种无痕迹,可逆的蛋白质PEGylation试剂,利用酸化学.

主要方法:

  • 合成和表征具有不同硬质环境的硫化合物.
  • 动力学研究,以评估酸链接的反应性和可调性.
  • 开发和测试一种基于硫化学的新型蛋白质PEGylation试剂.

主要成果:

  • 与二硫化物相比,Thioester表现出易于合成和一个数量级更大的动态可调性.
  • 通过调整体体围绕体结合的体积,可以精确调节体的活性.
  • 一种新的无痕和可逆的蛋白质PEGylation试剂成功地使用硫化学开发出来.

结论:

  • 泰奥斯特化学代表了一种多功能和高度可调的平台,用于开发下一代减少响应药物递送系统.
  • 蒂奥的简单合成和广泛的动力控制克服了当前基于二硫化物的方法的局限性.
  • 开发的基于铁的PEGylation试剂显示了对先进的生物结合策略的希望.