Laboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy.
Department of Chemistry, University of Richmond, Richmond, VA 23173, USA.
Life (Basel). 2013 Feb 5;3(1):149-60. doi: 10.3390/life3010149.
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.
来自嗜热古菌 Thermotoga maritima 的精氨酸结合蛋白是一种 27.7 kDa 的蛋白质,具有典型的周质结合蛋白家族的两域结构。该蛋白的特点是对精氨酸具有非常高的特异性和亲和力,即使在高温下也是如此。由于其特性,这种蛋白可以被考虑作为设计用于检测精氨酸的生物传感器的潜在候选物。当用于生物技术应用时,研究蛋白质的稳定性非常重要。本文综述了来自极端嗜热古菌 Thermotoga maritima 的一种精氨酸结合蛋白的结构和功能特征,特别关注其在生物技术应用中的潜在应用。