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.
Copyright © 2013 MDPI AG. This article first appeared in Life 3:1 (2013), 149-160.
Please note that downloads of the article are for private/personal use only.
Ausili, Alessio, Maria Staiano, Jonathan Dattelbaum, Antonio Varriale, Alessandro Capo, and Sabato D'auria. "Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga Maritima: A Brief Thermo-Story." Life 3, no. 1 (2013): 149-160. doi:10.3390/life3010149.