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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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Main Authors: | , , , , , |
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Formato: | Artigo |
Idioma: | Inglês |
Publicado em: |
Public Library of Science (PLoS)
2014-01-01
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Colecção: | PLoS ONE |
Acesso em linha: | http://europepmc.org/articles/PMC4022495?pdf=render |
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