A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima.

A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima.

The arginine binding protein from Thermatoga maritima (TmArgBP), a substrate binding protein (SBP) involved in the ABC system of solute transport, presents a number of remarkable properties. These include an extraordinary stability to temperature and chemical denaturants and the tendency to form mul...

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Bibliographic Details
Main Authors: Alessia Ruggiero, Jonathan D Dattelbaum, Maria Staiano, Rita Berisio, Sabato D'Auria, Luigi Vitagliano
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4022495?pdf=render

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http://europepmc.org/articles/PMC4022495?pdf=render

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