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Main description:
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cofactors have not yet been discovered, although there seem to be GimC-like homologs in some archaeal species (unpublished obs- vations by M. Leroux).
Contents:
Purification of Archaeal Chaperonin from Sulfolobus shibatae, Elsie Quaite-Randall and Andrzej Joachimiak. Purification of Hsp60 from Thermus thermophilus, Elsie Quaite-Randall and Andrzej Joachimiak. Purification of GroEL from an Overproducing E. coli Strain, Elsie Quaite-Randall and Andrzej Joachimiak. Purification of GroES from an Overproducing E. coli Strain, Elsie Quaite-Randall and Andrzej Joachimiak. Purification of the Gp31 Co-chaperonin from Bacteriophage T4, Saskia M. van der Vies. Removing Trace Fluorescent Contaminants from GroEL Preparations, Frank Weber. Assembly and Disassembly of GroEL and GroES Complexes, Joerg Martin. GroEL/GroES Interaction Assayed by Protease Protection, Joerg Martin. Determination of Chaperonin Activity In Vivo, Saskia M. van der Vies and Peter A. Lund. Interaction of Nonnative Polypeptide Substrates with the Escherichia coli Chaperonin GroEL, Wanda K. Hartmann and Edward Eisenstein. Prevention of Rhodanese Aggregation by the Chaperonin GroEL, Frank Weber and Manajit Hayer-Hartl. Refolding of Bovine Mitochondrial Rhodanese by Chaperonins GroEL and GroES, Frank Weber and Manajit Hayer-Hartl. Assay of Malate Dehydrogenase: A Substrate for the E. coli Chaperonins GroEL and GroES, Manajit Hayer-Hartl. Assay of Chaperonin-Assisted Refolding of Citrate Synthase, N. Kalaya Steede, Stacy L. Temkin, and Samuel J. Landry. Purification of Yeast Mitochondrial Hsp60, Yves Dubaquie, Renate Looser, and Sabine Rospert. Preparation of Recombinant Hsp10, N. Kalaya Steede, Jesse J. Guidry, and Samuel J. Landry. Purification of the Cytosolic Chaperonin TRiC from Bovine Testis, Raul G. Ferreyra and Judith Frydman. Monitoring Actin Folding: Purification Protocols for Labeled Proteins and Binding to DNase I-Sepharose Beads, Vanitha Thulasiraman, Raul G. Ferreyra, and Judith Frydman. Folding Assays: Assessing the Native Conformation of Proteins, Vanitha Thulasiraman, Raul G. Ferreyra, and Judith Frydman. Purification of Prefoldin, Sally A. Lewis andNicholas J. Cowan. Purification of GimC from Saccharomyces cerevisiae, Katja Siegers and Elmar Schiebel. Analysis of Eukaryotic Molecular Chaperone Complexes Involved in Actin Folding, Michel R. Leroux. Index
PRODUCT DETAILS
Publisher: Springer (Humana Press Inc.)
Publication date: November, 2010
Pages: 224
Weight: 740g
Availability: Available
Subcategories: Biochemistry
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