disulfide

简明释义

英[daɪˈsʌlfaɪd]美[daɪˈsʌlfaɪd]

n. [无化]二硫化物（等于 disulphide）

英英释义

单词用法

同义词

反义词

例句

1.Exposure to industrial or environmental chemicals such as carbon monoxide or carbon disulfide can also have this effect.

暴露于工业或环境化学品如一氧化碳或二硫化碳也可以有这种效果。

2.Objective to study the effect of carbon disulfide infection of mice myocardial cell apoptosis.

目的探讨二硫化碳染毒对小鼠心肌细胞凋亡的影响。

3.So if we get rid of the carbon disulfide and put CHCl3 in there, that's more favorable.

那么如果我们把二硫化碳去掉，换成CHCl3，则更有利。

4.Diallyl disulfide is not the most potent compound found in garlic, but it has an advantage because it is the less volatile of the compounds.

Diallyl disulfide二硫化物在大蒜中不是最有效的复合物，但是因为他在复合物中不易挥发，具有优势。

5.The disulfide Bridges are formed selectively after isolation, and the final purification is effected by chromatographic procedures.

二硫键形成的选择性分离后，最终由色谱净化工序的影响。

6.The research is enclosed the reaction between ammonia and carbon disulfide in the synthesis of ammonium thiocyanate.

论文研究是围绕以二硫化碳和氨为原料合成硫氰酸铵的反应过程进行的。

7.Methods of disulfide formation in peptide synthesis are reviewed in this paper.

综述了多肽合成中几种形成二硫键的方法。

8.It is insoluble in ethanol and carbon disulfide.

不溶于乙醇和二硫化碳。

9.The protein's structure is stabilized by the formation of disulfide bonds.

这种蛋白质的结构通过形成二硫键而稳定。

10.In some enzymes, disulfide linkages play a crucial role in maintaining activity.

在一些酶中，二硫键连接在维持活性方面起着至关重要的作用。

11.The cosmetic product claims to enhance hair strength through disulfide bond repair.

这款化妆品声称通过修复二硫键来增强头发的强度。

12.Researchers are studying how disulfide bonds affect protein folding.

研究人员正在研究二硫键如何影响蛋白质折叠。

13.The reduction of disulfide bonds can lead to protein denaturation.

还原二硫键可能导致蛋白质变性。

作文

The world of chemistry is filled with fascinating compounds and structures, one of which is the disulfide (二硫化物). This unique chemical bond plays a critical role in the stability and functionality of various biological molecules, particularly proteins. Understanding the significance of disulfide bonds can provide insights into the intricate nature of life itself. A disulfide bond is formed when two sulfur atoms from different cysteine residues in a protein come together, creating a covalent linkage. This process occurs through an oxidation reaction where hydrogen atoms are removed, allowing the sulfur atoms to bond. The formation of disulfide bonds is essential for the proper folding of proteins, as they help maintain the three-dimensional structure that is crucial for a protein's function. For instance, consider the protein insulin, which regulates blood sugar levels in the body. Insulin consists of two peptide chains linked by disulfide bonds, ensuring its stability and functionality. If these disulfide bonds were disrupted, insulin would lose its structural integrity, leading to severe metabolic disorders. This example illustrates how vital disulfide bonds are in maintaining the biological activity of proteins. Moreover, disulfide bonds are not only significant in human biology but also play a crucial role in various industrial applications. In the production of rubber, for example, disulfide linkages contribute to the elasticity and strength of the material. The vulcanization process, which involves heating rubber with sulfur, creates disulfide bonds that enhance the properties of rubber, making it suitable for a wide range of products, from tires to footwear. In addition to their structural importance, disulfide bonds are also involved in cellular signaling processes. They can act as redox sensors, responding to changes in the cellular environment. When oxidative stress occurs, the formation of new disulfide bonds can signal the activation of specific pathways that help protect cells from damage. This dual role of disulfide bonds—structural and regulatory—highlights their complexity and importance in both biology and industry. Despite their significance, disulfide bonds can also pose challenges. For example, in the pharmaceutical industry, the presence of disulfide bonds in therapeutic proteins can complicate their production and storage. The stability of these proteins can be affected by environmental factors such as temperature and pH, which may lead to the breakage of disulfide bonds and loss of functionality. Therefore, understanding how to manipulate and stabilize disulfide bonds is crucial for developing effective biopharmaceuticals. In conclusion, the disulfide bond (二硫化物) is a fundamental component in the realm of chemistry and biology. Its ability to stabilize protein structures, contribute to industrial materials, and participate in cellular signaling emphasizes its multifaceted roles. As we continue to explore the complexities of life at the molecular level, the study of disulfide bonds will undoubtedly remain a key area of interest for scientists and researchers alike.