Allostery是一个生物学术语，指一个细胞器或分子通过与一个配体结合，使另一个在一定距离之外的结合位点发生功能改变的现象。
以下是一篇关于allostery的英文范文，希望对你有所帮助。
Title: Allostery: A Mechanism of Protein Functionality Over Distance
Allostery is a fascinating phenomenon in biology, where a protein's functionality is altered by a binding event at a site remote from the binding site that directly interacts with a traditional ligand. This binding event can occur in the absence of a traditional ligand, and it is thought to be the mechanism by which proteins can maintain their functionality over long distances.
In recent years, allostery has been studied extensively in the context of the immune system, where antibodies are particularly interesting due to their ability to recognize and bind to foreign proteins with exquisite specificity. In antibodies, allostery has been shown to play a crucial role in maintaining the structure and functionality of the antibody during binding, and it has even been proposed as a potential target for therapeutic intervention.
Here, we present an example of allostery in action using data from a recent study on antibodies. We show how a binding event at one site on an antibody can affect the functionality of another site on the same antibody, over a distance of several hundred amino acids. This phenomenon highlights the remarkable ability of allostery to maintain protein functionality over long distances, and it emphasizes its potential as a target for therapeutic intervention.
总的来说，allostery是一种蛋白质功能改变的现象，通过与一个配体结合，一个细胞器或分子可以使另一个在一定距离之外的结合位点发生功能改变。这是一个非常有趣和复杂的生物学现象，在蛋白质功能的研究中具有重要意义。
allostery是一个生物学词汇，指的是蛋白质结构中远离活性中心的部位与功能变化有关，这种变化是由蛋白质分子内部或与其他分子（如配体、金属离子）之间的相互作用引起的。
在英文范文当中，allostery常常被用于描述特定蛋白质结构或机制如何利用周围环境中的变化来调节其功能。此外，allostery也常用于描述生物系统中，信息从一个结构域（通常是远离活性中心的部位）传递到另一个结构域，从而影响整个系统的行为。
allostery是指蛋白质结构中，非活性位点上的变化通过影响活性位点的结构或功能，而引起的蛋白质活性变化的现象。
以下是一篇关于allostery的英文范文最新变化：
Allostery: A Key to Protein Function
In biology, allostery refers to a phenomenon where the activity of a protein is modulated by changes in a region of the protein that is not the binding site for a ligand (the “allosteric site”). This type of modulation can have profound effects on the protein’s function and is thought to be critical in many biological processes.
In recent years, allostery has become an area of intense research interest because of its potential to provide new insights into the mechanisms of protein function and regulation. This interest has been fueled by advances in biotechnology and high-throughput screening methods that have made it possible to study large numbers of proteins and their allosteric interactions.
Moreover, the development of computational methods for modeling allosteric mechanisms has enabled researchers to gain a deeper understanding of these complex processes. These methods have been instrumental in identifying key allosteric signatures and in developing new approaches for predicting protein function and design.
Overall, allostery represents a key concept in modern biology that has opened up new avenues for research and discovery in the field of protein science.