antiparallel beta structure

简明释义

逆平行结构

英英释义

例句

1.The antiparallel beta structure (反平行β结构) plays a vital role in the formation of amyloid fibrils associated with diseases.

在与疾病相关的淀粉样纤维的形成中，反平行β结构（antiparallel beta structure）起着至关重要的作用。

2.The antiparallel beta structure (反平行β结构) is often found in the core of globular proteins, providing them with structural integrity.

在球状蛋白的核心中常常发现反平行β结构（antiparallel beta structure），为它们提供了结构完整性。

3.Research has shown that the antiparallel beta structure (反平行β结构) is crucial for the function of many enzymes.

研究表明，反平行β结构（antiparallel beta structure）对许多酶的功能至关重要。

4.The protein's stability is significantly influenced by the presence of an antiparallel beta structure (反平行β结构) in its secondary conformation.

蛋白质的稳定性受到其二级构象中存在的反平行β结构（antiparallel beta structure）的显著影响。

5.In structural biology, the identification of an antiparallel beta structure (反平行β结构) can help predict protein interactions.

在结构生物学中，识别反平行β结构（antiparallel beta structure）可以帮助预测蛋白质相互作用。

作文

In the intricate world of molecular biology, the understanding of protein structures is fundamental to grasping how life functions at a cellular level. One of the most fascinating aspects of protein architecture is the formation of secondary structures, particularly the antiparallel beta structure. This term refers to a specific arrangement of beta strands in a protein's secondary structure, where adjacent strands run in opposite directions. The significance of this configuration lies not only in its stability but also in its role in the overall functionality of proteins.The antiparallel beta structure consists of beta strands that are connected by hydrogen bonds, forming a sheet-like structure. These strands are typically around five to ten amino acids in length and are aligned such that the N-terminus of one strand is adjacent to the C-terminus of another. This orientation allows for optimal hydrogen bonding between the carbonyl oxygen of one strand and the amide hydrogen of another, providing greater stability compared to parallel beta structures. The unique arrangement of these strands can be visualized as arrows pointing in opposite directions, hence the name 'antiparallel'.Understanding the antiparallel beta structure is crucial for several reasons. First, it contributes significantly to the overall stability of proteins. The extensive hydrogen bonding network formed in this configuration helps to maintain the integrity of the protein's three-dimensional shape, which is essential for its biological activity. Proteins are often required to adopt specific shapes to interact with other molecules, and any disruption in their structure can lead to loss of function or even diseases.Moreover, the antiparallel beta structure is prevalent in many important proteins, including enzymes and structural proteins. For instance, silk fibroin, a protein produced by silkworms, is primarily composed of this structure. The strength and durability of silk are attributed to the extensive antiparallel beta structures within its molecular framework. Similarly, many enzymes that catalyze biochemical reactions exhibit this structure, highlighting its importance in enzymatic activity and efficiency.Another interesting aspect of the antiparallel beta structure is its role in protein folding. During the process of protein synthesis, polypeptide chains fold into specific three-dimensional configurations, and the formation of antiparallel beta structures is a critical step in this process. Misfolded proteins, which may result from errors during synthesis or external factors, can lead to various diseases, including Alzheimer's and Parkinson's. By studying the formation of these structures, researchers can gain insights into the mechanisms of protein misfolding and develop potential therapeutic strategies.In conclusion, the antiparallel beta structure is a vital component of protein architecture that plays a significant role in determining the stability and functionality of proteins. Its unique arrangement allows for optimal hydrogen bonding, contributing to the overall integrity of protein structures. As we continue to explore the complexities of molecular biology, understanding structures like the antiparallel beta structure will be essential in advancing our knowledge of life at the molecular level and addressing challenges related to protein misfolding and associated diseases.

在分子生物学的复杂世界中，理解蛋白质结构对于掌握生命在细胞层面的功能至关重要。蛋白质结构的一个最迷人的方面是二级结构的形成，特别是反平行β结构。这个术语指的是蛋白质二级结构中β链的特定排列，其中相邻的链沿相反方向运行。这种配置的重要性不仅在于其稳定性，还在于其在蛋白质整体功能中的作用。反平行β结构由通过氢键连接的β链组成，形成类似于薄片的结构。这些链通常长度在五到十个氨基酸之间，并且排列方式使得一条链的N端与另一条链的C端相邻。这种取向允许最佳的氢键结合，即一条链的羰基氧与另一条链的酰胺氢之间的结合，从而提供比平行β结构更大的稳定性。这些链的独特排列可以被想象成箭头指向相反的方向，因此得名“反平行”。理解反平行β结构至关重要，原因有几个。首先，它对蛋白质的整体稳定性贡献显著。该配置形成的广泛氢键网络有助于维持蛋白质三维形状的完整性，这对其生物活性至关重要。蛋白质通常需要采用特定形状以与其他分子相互作用，而任何结构的破坏都可能导致功能丧失或甚至疾病。此外，反平行β结构在许多重要蛋白质中普遍存在，包括酶和结构蛋白。例如，丝素蛋白是蚕产生的一种蛋白质，其主要由这种结构组成。丝绸的强度和耐用性归因于其分子框架中的广泛反平行β结构。同样，许多催化生化反应的酶也表现出这种结构，突显了它在酶活性和效率中的重要性。反平行β结构的另一个有趣方面是它在蛋白质折叠中的作用。在蛋白质合成过程中，多肽链折叠成特定的三维配置，而反平行β结构的形成是这一过程中的关键步骤。错误折叠的蛋白质可能是由于合成过程中的错误或外部因素引起的，可能导致各种疾病，包括阿尔茨海默病和帕金森病。通过研究这些结构的形成，研究人员可以深入了解蛋白质错误折叠的机制，并开发潜在的治疗策略。总之，反平行β结构是蛋白质结构的重要组成部分，在决定蛋白质的稳定性和功能性方面发挥着重要作用。其独特的排列方式允许最佳的氢键结合，有助于蛋白质结构的整体完整性。随着我们继续探索分子生物学的复杂性，理解像反平行β结构这样的结构将对推进我们对分子层面生命的知识以及解决与蛋白质错误折叠和相关疾病的问题至关重要。