Image from Google Jackets

Chaperonin Protocols / edited by Christine Schneider

Material type: materialTypeLabelE-bookSeries: (Methods in Molecular Biology, 1940-6029; 140).Publisher: Totowa, NJ : Humana Press, 2000Edition: 1st edition 2000.Description: 1 recurso en línea (X, 212 páginas).ISBN: 9781592590612.Subject: Bioquímica | Biología molecularOnline resources: Acceso a este recurso digital (usuarios Universidad Europea de Madrid)Digital Resources
Contents:
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.
Summary: 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.
Tags from this library: No tags from this library for this title. Log in to add tags.
Star ratings
    Average rating: 0.0 (0 votes)
Holdings
Item type Current library Collection Call number Status Date due Barcode Item holds
LIBRO-E NO PRÉSTAMO LIBRO-E NO PRÉSTAMO Madrid Digital Acceso Electrónico (UEM) Ciencias de la Salud QP552 .M64 2000 EB (Browse shelf(Opens below)) Acceso electrónico eBook.20123859
Total holds: 0

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.

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.

There are no comments on this title.

to post a comment.
Share