2013

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

Life (Basel, Switzerland) Ausili A, Staiano M, Dattelbaum J, Varriale A, Capo A, D'Auria S
阅读原文 PDF DOI PubMed

组成图示

示意图生成中

传感器类型

检测对象

检测原理

检测灵敏度

效应效果

传感器的构成

中文摘要

英文摘要

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.

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