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相关概念视频

Protein Folding01:25

Protein Folding

8.1K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.1K
Protein and Protein Structure02:15

Protein and Protein Structure

79.8K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
79.8K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.3K
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...
5.3K
Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.6K
Protein Organization01:24

Protein Organization

6.6K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
6.6K
Peptide Bonds02:43

Peptide Bonds

74.8K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
74.8K

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The B. subtilis replicative polymerases bind the sliding clamp with different strengths to tune their activity in DNA replication.

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相关实验视频

Updated: Jul 25, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

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折叠辅助二硫化物的形成和二聚化.

Clara G Victorio1, Nicholas Sawyer1

  • 1Department of Chemistry, Fordham University, 441 E. Fordham Rd., Bronx, New York 10458, United States.

ACS chemical biology
|June 30, 2023
PubMed
概括

控制醇氧化条件允许选择性地在中形成二硫化键. 这种方法可以产生单体或二元物种,影响折叠和稳定性,用于各种应用.

科学领域:

  • 生物化学和分子生物学
  • 化学合成和化学化学

背景情况:

  • 二硫化键是和蛋白质中的关键共价连接,显著影响它们的结构,稳定性和寡合化.
  • 控制二硫化物键形成对于理解和设计和蛋白质折叠至关重要,特别是在化学合成分子中.

研究的目的:

  • 为了研究不同硫醇氧化条件如何影响线性比斯蒂醇的折叠和寡合化.
  • 展示一种控制中特定二硫化物键结构 (单与二) 的形成的方法.

主要方法:

  • 通过完全无保护的线性比斯蒂醇的受控氧化,选择性地形成二硫化键.
  • 在水中 (非自然化) 与非自然化氧化条件下形成的类的比较分析.
  • 评估变异,以确定影响分子内二硫化物形成和二聚化的因素.

主要成果:

  • 一个p53衍生的的非自然化水性氧化产生了增加α-螺旋含量的反平行二元体.
  • 变性氧化条件有利于形成非螺旋型分子内二硫化物种.
  • 内部分子二硫化物形成在不同的序列中被证明是稳健的,而二聚化则取决于螺旋折叠和芳香残留.

结论:

  • 醇氧化条件可以在战略上使用,以控制通过二硫化键形成的类寡合化和折叠.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

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相关实验视频

Last Updated: Jul 25, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

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  • 由此产生的二硫酸结合与线性对应物相比,表现出增强的蛋白酶抗性.
  • 这种方法为研究折叠,寡合化和与分子标相互作用提供了一种多功能工具.