• Abstract
• Full-Text PDF [551 KB]
• Full-Text XML
• Article Versions Notes

• Article Statistics
• Google Scholar
• Order Reprints

• Cite this article
• Export to BibTeX
• Export to EndNote

• [+] on DOAJ
• Ausili, A
• Staiano, M
• Dattelbaum, J
• Varriale, A
• Capo, A
• D'Auria, S
• [+] on Google Scholar
• Ausili, A
• Staiano, M
• Dattelbaum, J
• Varriale, A
• Capo, A
• D'Auria, S
• [+] on PubMed
• Ausili, A
• Staiano, M
• Dattelbaum, J
• Varriale, A
• Capo, A
• D'Auria, S

•  CiteULike
•  Facebook
•  Mendeley
•  Twitter

This article is

• freely available
• re-usable

Life 2013, 3(1), 149-160; doi:10.3390/life3010149

Review

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

Alessio Ausili ¹ , Maria Staiano ¹ , Jonathan Dattelbaum ² , Antonio Varriale ¹ , Alessandro Capo ¹  and Sabato D'Auria ^1,*

¹ Laboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy ² Department of Chemistry, University of Richmond, Richmond, VA 23173, USA

* Author to whom correspondence should be addressed.

Received: 16 November 2012; in revised form: 11 January 2013 / Accepted: 29 January 2013 / Published: 5 February 2013

(This article belongs to the Special Issue Extremophiles and Extreme Environments)

Download PDF Full-Text [551 KB, uploaded 5 February 2013 09:45 CET]

Abstract: 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.

Keywords: ABC transporters; periplasmic binding proteins; arginine; structural stability; unfolding

Article Statistics

Cite This Article