Humana Chaperonin Protocols: 140 (Methods in Molecular Biology, 140)

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cofactors have not yet been discovered, although there seem to be GimC-like homologs in some archaeal species (unpublished obs- vations by M. Leroux). Review "This book is highly recommended for academic libraries and for those special or industrial libraries that support a program in microbiology. Because the clear and logical approach to each protocol can serve as a model experiment that is easily reproduced, this book would be an especially valuable tool for students."-E-Streams (Electronic Reviews of Science and Technology References) "...an invaluable overview of two main aspects of chaperonin research-purification of chaperonins and their cofactors and assays to monitor folding activity. ...of excellent chapters on more diverse chaperonins, including those from Archaea and the specialized, eukaryotic TRiC complex....The book provides a wealth of explicitly detailed protocols (together with useful troubleshooting notes) for all those working in the field of chaperonins and protein folding or misfolding."...Microbiology Today From the Back Cover In Chaperonin Protocols, Christine Schneider has assembled a unique collection of readily reproducible protocols for the study of chaperonins, intracellular proteins critical to many biological processes. Written by experienced investigators who have successfully honed their methods to a fineness, the protocols focus on the purification of chaperonins from different species along with their corresponding cofactors, and on chaperonin activity assays for in vivo as well as in vitro work. Many activity assays are given for GroEL, which can also be applied to mitochrondrial Hsp60. There are also assays for the eukaryotic chaperonin TRiC and handy methods-for example, one for preparing labeled probes-that can be used for various purposes and prove helpful in numerous different procedures. Critically important to a greater understanding of such disorders as cystic fibrosis, Alzheimer's disease, and BSE, Chaperonin Protocols offers both novice and experienced investigators fast access to today's best and most productive chaperonin methods, all explained in step-by-step detail to ensure robust and reproducible results.