Titlebook: Chaperonin Protocols; Christine Schneider Book 2000 Humana Press 2000

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Purification of GroEL from an Overproducing E. coliStrain,ical domain and is sequestered inside the cavity of the chaperonin owing to the binding of the cochaperonin, GroES, to the same sites on the apical domains. Release of the protein from the chaperonin occurs after ATP hydrolysis. Chaperonins are broadly further classified into two other groups based

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Purification of the Gp31 Co-chaperonin of BacteriophageT4, of Gp31, indicating that the Gp31 protein possesses distinct properties that are absent in GroES (.-.). The 2.3-Å crystal shows that the tertiary and quaternary structures of the Gp31 heptamer are similar to those of GroES, despite the low amino acid sequence identity between the two proteins (14%)

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Narrative

GroEL/GroES Interaction Assayed by Protease Protection,t of the cylinder cavity, as shown by the fact that a carboxy-terminally His-tagged GroEL is able to bind to Ni-NTA affinity columns (.). Second, proteinase K (29 kDa) is small enough to enter the cavity and to exert its proteolytic activity there.

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Interaction of Nonnative Polypeptide Substrates with the Escherichia coli Chaperonin GroEL, partitions to GroEL from solution. Some of these methods have relied on the heat exchanged on polypeptide binding to GroEL (., .), on the distribution of bound and free substrates detected by ultracen- trifugation (., .), and on changes in surface plasmon resonance using BIAcore (., .) .). . (.,.,

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Monitoring Actin Folding, of [.S]-labeled purified actin. We include a protocol to purify [.S]-labeled actin overexpressed in bacterial cells. This protocol can be used to purify any other labeled protein following overexpression in bacteria, including luciferase and tubulin. We also describe a protocol to purify [.S]-label

蛰伏

Assay of Malate Dehydrogenase,okaryotes contain only a single form of MDH. The crystal structures of MDH from . (..), porcine cytoplasm (.), porcine mitochondria (..), and . (.) have been solved and are essentially identical. Refer to ref. (.) for a comprehensive review on MDH.

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Christine SchneiderIncludes supplementary material: