通过selenoxo光开关调节骨形状的调节
Yun Huang1, Günther Jahreis, Christian Lücke
1Max-Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany.
Journal of the American Chemical Society
|May 21, 2010
概括
研究人员开发了稳定的素,允许使用紫外线光照对脊柱形状进行光控制. 这使得监测异构体特定的生物化学反应,由于长期存在的非平衡状态.
科学领域:
- 生物化学 生物化学
- 有机化学 有机化学
- 摄影化学的使用.
背景情况:
- 通过外部信号控制和蛋白质生物活性至关重要.
- 脊柱形状的光控制提供了一个新的调节机制.
研究的目的:
- 将类型的类型的键引入到四甲中.
- 为了研究由此产生的的光控制能力和稳定性.
- 评估监测异构体特定生物化学反应的潜力.
主要方法:
- 合成含有一种类型的类型键 (氧键) 的四甲.
- 用近290nm的紫外线照射素的辐射.
- 在光静态状态下分析cis含量.
- 对热再平衡率的监测.
主要成果:
- 取得了令人惊的稳定的.
- 在紫外线照射时,链中cis含量显著增加.
- 观察到缓慢的热再平衡,速度常数表明长期存在的非平衡形状.
结论:
- 素提供了一个强大的平台,用于光控制脊柱形状.
- 长期存在的过渡形状使生物化学反应中异构体特异性的研究更容易.
- 这种方法为生物分子功能的外部信号介导调节提供了新的可能性.
相关概念视频
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.
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 Folding
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...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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.
These groups modify specific amino acids in a protein.
Protein and Protein Structure
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 can...
A protein's shape is critical to its function. For example, an enzyme can...
Preparation and Reactions of Sulfides
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.


