allosteric transition

简明释义

变构转变

英英释义

例句

1.The allosteric transition is crucial for the regulation of many biochemical pathways.

对于许多生化途径的调节来说，别构转变至关重要。

2.The enzyme exhibited an allosteric transition that enhanced its activity in response to substrate binding.

该酶表现出一种别构转变，在底物结合时增强其活性。

3.Researchers are studying the allosteric transition of hemoglobin to explain its oxygen-binding properties.

研究人员正在研究血红蛋白的别构转变以解释其氧结合特性。

4.Inhibitors can affect the allosteric transition, leading to decreased enzyme activity.

抑制剂可以影响别构转变，导致酶活性降低。

5.Understanding the allosteric transition can help in designing better drugs for metabolic disorders.

理解别构转变有助于设计更好的药物用于代谢障碍。

作文

The concept of allosteric transition is crucial in understanding how enzymes and proteins function in biological systems. In simple terms, allosteric transition refers to a change in the shape or conformation of a protein that occurs when a molecule binds to a site other than the active site. This binding can lead to a functional change in the protein, either enhancing or inhibiting its activity. The term 'allosteric' comes from the Greek word 'allos', meaning 'other', and 'stereos', meaning 'solid' or 'shape'. Thus, it literally translates to 'other shape'.Proteins are made up of long chains of amino acids that fold into specific three-dimensional structures. These structures are essential for the protein's function. When a substrate or an effector molecule binds to a protein, it can induce a allosteric transition, altering the protein's configuration. This alteration can affect how the protein interacts with other molecules, thereby playing a significant role in various biochemical pathways.One of the most well-known examples of allosteric transition is found in hemoglobin, the protein responsible for transporting oxygen in the blood. Hemoglobin exhibits cooperative binding, which is a type of allosteric transition. When one molecule of oxygen binds to hemoglobin, it causes a conformational change that increases the affinity of the remaining binding sites for oxygen. This means that as more oxygen molecules bind to hemoglobin, it becomes progressively easier for additional oxygen to attach. This mechanism is vital for efficient oxygen transport and release in the body.Another important aspect of allosteric transition is its role in enzyme regulation. Many enzymes are regulated by allosteric effectors, which can be either activators or inhibitors. Activators promote the enzyme's activity by stabilizing the active form of the enzyme, while inhibitors stabilize the inactive form. This regulation allows cells to respond dynamically to changes in their environment, ensuring that metabolic processes are finely tuned to meet cellular needs.The study of allosteric transition has significant implications in drug design and therapeutic interventions. By targeting allosteric sites on proteins, researchers can develop drugs that modulate protein activity without directly competing with the substrate. This approach can lead to more selective and potentially less toxic treatments. For instance, allosteric modulators are being explored in the context of cancer therapy, where they can help to restore normal function to mutated proteins involved in cell growth and division.In conclusion, the concept of allosteric transition is fundamental to our understanding of protein function and regulation. It highlights the intricate ways in which proteins can change their shape and activity in response to different signals. As research continues to explore the mechanisms underlying allosteric transition, we gain deeper insights into the complexities of biological systems and the potential for innovative therapeutic strategies. The ability of proteins to undergo such transitions underscores the elegance of molecular biology and the sophistication of life at the cellular level.

“变构转变”这一概念对于理解酶和蛋白质在生物系统中的功能至关重要。简单来说，“变构转变”指的是当一个分子结合到活性位点以外的地方时，蛋白质的形状或构象发生变化。这种结合可以导致蛋白质的功能变化，增强或抑制其活性。“变构”一词源于希腊语“allos”，意为“其他”，以及“stereos”，意为“固体”或“形状”。因此，它字面意思是“其他形状”。蛋白质由长链氨基酸组成，这些氨基酸折叠成特定的三维结构。这些结构对蛋白质的功能至关重要。当底物或效应分子结合到蛋白质上时，它可能会诱导“变构转变”，改变蛋白质的构型。这种改变可以影响蛋白质与其他分子的相互作用，从而在各种生化途径中发挥重要作用。“变构转变”的一个著名例子是在血红蛋白中，血红蛋白是负责运输氧气的蛋白质。血红蛋白表现出协同结合，这是一种“变构转变”。当一个氧分子结合到血红蛋白时，会引起构象变化，从而增加其余结合位点对氧气的亲和力。这意味着，随着更多氧分子的结合，附加氧气变得更加容易。这一机制对身体内高效的氧气运输和释放至关重要。“变构转变”的另一个重要方面是它在酶调节中的作用。许多酶通过变构效应因子进行调节，这些效应因子可以是激活剂或抑制剂。激活剂通过稳定酶的活性形式来促进酶的活性，而抑制剂则稳定酶的不活性形式。这种调节使细胞能够动态响应环境的变化，确保代谢过程精细调整以满足细胞需求。对“变构转变”的研究在药物设计和治疗干预中具有重要意义。通过靶向蛋白质的变构位点，研究人员可以开发出调节蛋白质活性的药物，而无需直接与底物竞争。这种方法可以导致更具选择性且潜在毒性较低的治疗。例如，在癌症治疗中，正在探索变构调节剂，它们可以帮助恢复参与细胞生长和分裂的突变蛋白的正常功能。总之，“变构转变”的概念是我们理解蛋白质功能和调节的基础。它突显了蛋白质如何以不同信号响应而改变其形状和活性。随着研究继续探索“变构转变”背后的机制，我们对生物系统复杂性的理解不断加深，以及创新治疗策略的潜力。蛋白质经历这种转变的能力强调了分子生物学的优雅性和细胞层面生命的复杂性。