Two-dimensional IR correlation spectroscopy of mutants of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events

β-Glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus is a homotetramer with a higher number of ion pairs compared with mesophilic glycoside hydrolases. The ion pairs are arranged in large networks located mainly at the tetrameric interface of the molecule. In the present study,...

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Hlavní autoři: Ausili, Alessio, Di Lauro, Barbara, Cobucci-Ponzano, Beatrice, Bertoli, Enrico, Scirè, Andrea, Rossi, Mosè, Tanfani, Fabio, Moracci, Marco
Médium: Artigo
Jazyk:Inglês
Vydáno: Portland Press Ltd. 2004
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Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1134089/
https://ncbi.nlm.nih.gov/pubmed/15283674
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20040646
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