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Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story

机译:嗜热菌中的周质结合蛋白:海栖嗜热菌精氨酸结合蛋白的表征和潜在应用:简要的热故事

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摘要

Arginine-binding protein from the extremophile Thermotoga maritima is a 27.7 kDa protein possessing the typical two-domain structure of the periplasmic binding proteins family. The protein is characterized by a very high specificity and affinity to bind to arginine, also at high temperatures. Due to its features, this protein could be taken into account as a potential candidate for the design of a biosensor for arginine. It is important to investigate the stability of proteins when they are used for biotechnological applications. In this article, we review the structural and functional features of an arginine-binding protein from the extremophile Thermotoga maritima with a particular eye on its potential biotechnological applications.
机译:来自极端嗜热菌(Thermotoga maritima)的精氨酸结合蛋白是一种27.7 kDa的蛋白,具有周质结合蛋白家族的典型两个结构域结构。该蛋白质的特征还在于在高温下也具有非常高的特异性和与精氨酸结合的亲和力。由于其特征,该蛋白质可以被认为是设计精氨酸生物传感器的潜在候选者。当蛋白质用于生物技术应用时,研究其稳定性非常重要。在本文中,我们将审视极端微生物嗜热菌(Thermotoga maritima)的精氨酸结合蛋白的结构和功能特征,并特别关注其潜在的生物技术应用。

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