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  • Produktbild: Chaperonin Protocols
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Chaperonin Protocols

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Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

10.11.2010

Abbildungen

X, 212 p.

Herausgeber

Christine Schneider

Verlag

Humana Press

Seitenzahl

212

Maße (L/B/H)

22,9/15,2/1,3 cm

Gewicht

336 g

Sprache

Englisch

ISBN

978-1-61737-163-9

Beschreibung

Rezension

"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

Portrait

Christine Schneider, Stuttgart (BW), ist Diplom-Biologin mit Schwerpunkt Botanik und Lektorin für Naturführer und Fachbücher.

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

10.11.2010

Abbildungen

X, 212 p.

Herausgeber

Christine Schneider

Verlag

Humana Press

Seitenzahl

212

Maße (L/B/H)

22,9/15,2/1,3 cm

Gewicht

336 g

Sprache

Englisch

ISBN

978-1-61737-163-9

Herstelleradresse

Libri GmbH
Europaallee 1
36244 Bad Hersfeld
DE

Email: gpsr@libri.de

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  • Produktbild: Chaperonin Protocols
  • Produktbild: Chaperonin Protocols
  • 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.