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 Protein Folding in Archaea. Analysis of the Co-existing Group I and Group II Chaperonins in M. mazei
Наименование:

Protein Folding in Archaea. Analysis of the Co-existing Group I and Group II Chaperonins in M. mazei

издательство Книга по Требованию Другие общетехнические дисциплины
Cтраниц 208        мягкая обложка       
Аннотация:Chaperonins are divided into two distinct groups: the group I chaperonins in Bacteria (i. e. GroEL in E. coli) and group II chaperonins in Archaea and Eukaryotes. The barrel shaped chaperonins are a particular class of chaperones, they are absolutely essential and present in virtually every living cell. In vivo protein folding relies on assistance of so-called chaperones to guarantee a rapid and reliable adoption of the native state. In addition, the unique coexistence of both chaperonin groups in M. mazei allowed direct comparison of the substrate spectra of a bacterial and a eukaryo-typic folding machine. The correct three-dimensional structure of a protein is essential for its biological function. This study provides the first complete substrate spectrum of a group II chaperonin, the thermosome of the mesophilic archaeon Methanosarcina mazei. Substrate selection clearly differs among both chaperonin groups and is driven by a combination of physical properties, structural features and less defined characteristics such as the evolutionary status and the phylogenetic origin of the substrate protein.
Издательство: Книга по Требованию
Год:2008
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3233 руб
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Поиск: Protein Folding in Archaea. Analysis of the Co-existing Group I and Group II Chaperonins in M. mazei
НОВЫЙ ГОД СИМВОЛ 2013 ГОДАУКРАШЕНИЯ
КАРНАВАЛ НА НОВЫЙ ГОД РАСПРОДАЖА
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