Buch, Englisch, Band 140, 212 Seiten, Previously published in hardcover, Format (B × H): 152 mm x 229 mm, Gewicht: 336 g
Reihe: Methods in Molecular Biology
Buch, Englisch, Band 140, 212 Seiten, Previously published in hardcover, Format (B × H): 152 mm x 229 mm, Gewicht: 336 g
Reihe: Methods in Molecular Biology
ISBN: 978-1-61737-163-9
Verlag: Humana Press
The chaperonin field has captured the attention of numerous scientists in recent years. A rapidly increasing number of reviews and articles have tried to elucidate the mechanisms by which these multimeric complexes drive the fo- ing of newly synthesized and denatured proteins. An obvious common theme of chaperonin research first arose from the study of their structural features. All members of this class consist of multiple subunits that form cylindrical structures, which encage proteins in a cave-like environment where folding of proteins takes place according to the current view. Since the chaperonin structures are found even in very primitive org- isms, the archaebacteriae, this “cave scheme” seems to be an evolutionarily successful feature that was conserved and that appears among evolutionarily distinct organisms. Interestingly, almost all chaperonins have specific cofactors that are - volved in the folding process. Even for the eukaryotic cylinder TRiC or CCT, a cofactor called prefoldin or GimC was recently discovered. Only for the archaeal chaperonins cofactors have not yet been discovered, although there seem to be GimC-like homologs in some archaeal species (unpublished obs- vations by M. Leroux).
Zielgruppe
Research
Autoren/Hrsg.
Weitere Infos & Material
Purification of Archaeal Chaperonin from Sulfolobus shibatae.- Purification of Hsp60 from Thermus thermophilus.- Purification of GroEL from an Overproducing E. coliStrain.- Purification of GroES from an Overproducing E. coliStrain.- Purification of the Gp31 Co-chaperonin of BacteriophageT4.- Removing Trace Fluorescent Contaminants from GroEL Preparations.- Assembly and Disassembly of GroEL and GroES Complexes.- GroEL/GroES Interaction Assayed by Protease Protection.- Determination of Chaperonin Activity In Vivo.- Interaction of Nonnative Polypeptide Substrates with the Escherichia coli Chaperonin GroEL.- Prevention of Rhodanese Aggregation by the Chaperonin GroEL.- Refolding of Bovine Mitochondrial Rhodanese by Chaperonins GroEL and GroES.- Assay of Malate Dehydrogenase.- Assay of Chaperonin-Assisted Refolding of Citrate Synthase.- Purification of Yeast Mitochondrial Hsp60.- Preparation of Recombinant Human Hsp10.- Purification of the Cytosolic ChaperoninTRiC from Bovine Testis.- Monitoring Actin Folding.- Folding Assays.- Purification of Prefoldin.- Purification of GimC from Saccharomyces cerevisiae.- Analysis of Eukaryotic Molecular Chaperone Complexes Involved in Actin Folding.
