Molecular Chaperones, Volume 290

1st Edition

Serial Volume Editors: George Lorimer Thomas Baldwin
Print ISBN: 9780123917867
eBook ISBN: 9780080884028
Imprint: Academic Press
Published Date: 5th March 1998
Page Count: 500

Institutional Access


The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 285 volumes have been published (all of them still in print) and much of the material is relevant even today--truly an essential publication for researchers in all fields of life sciences.

Key Features

@introbul:Key Features @bul:* Catalysts of Protein Folding: Protein Disulfide Isomerases, Cis-trans Peptidyl Prolyl Isomerases

  • Accessory Proteins: Chaperonins, Cochaperonins, Pap Proteins, Sec Proteins
  • Physical methods for investigation of interactions between chaperones and their substances
  • Cotranslational protein folding, cell-free protein synthesis and associated methods


Cell biologists, geneticists, biochemists, biophysicists, and computational chemists.

Table of Contents

A.N. Fedorov and T.O. Baldwin, Protein Folding and Assembly in a Cell-Free Expression System.

B.A. Hardesty, G. Kramer, T. Zhang, and W. Kudlicki, Preparation and Application of Chaperone-Deficient Escherichia coli Cell-free Translation Systems.

H.F. Gilbert, V. McLean, and M. McLean, Protein Disulfide Isomerase.

Y. Yamada, S. Udaka, T. Kajino, C. Miyazaki, O. Asami, and M. Hirai, Thermophilic Fungal Protein Disulfide Isomerase.

J.C.A. Bardwell and T. Zander, Disulfide Bond Catalysts in Escherichia coli.

J.J. Siekierka and G. Wiederrecht, Yeast Immunophilins: Purification and Assay of Yeast FKBP12.

A.K. Matoo, Peptidylprolyl cis-trans-isomerases from Plant Organelles.

C. Frieden, A.C. Clark, and R. Ramanathan, Purification of GroEL with Low Fluorescence Background.

M. Fisher, E. Eisenstein, and P. Reddy, Overexpression, Purification, and Properties of GroES for Escherichia coli.

M.J. Todd and G.H. Lorimer, Criteria for Assessing the Purity and Quality of GroEL.

A.L. Horwich, S.G. Burston, H.S. Rye, J.S. Weissman, and W.A. Fenton, Construction of Single-Ring and Two-Ring Hybrid Versions of Bacterial Chaperonin GroEL.

B.A. McFadden and J.A. Torres-Ruiz, Chaperonin 6014 and Co-Chaperonin 107 from Chromatium vinosum.

F.R. Tabita, W.T. Lee, and G.M.F. Watson, Chaperonins of Purple Nonsulfur Bacterium Rhodobacter sphaeroides.

R.K. Scopes and K. Truscott, Chaperonins from Thermoanaerobacter Species.

M. Yoshida and H. Taguchi, Chaperonin from a Thermophile, Thermus thermophilus.

M. Morioka and H. Ishikawa, Insect Chaperonin 60: Symbionin.

G. Schatz, Y. Dubaquié,


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© Academic Press 1998
Academic Press
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About the Serial Volume Editor

George Lorimer

Affiliations and Expertise

E.I. Dupont De Nemours and Company, Wilmington, Delaware, U.S.A.

Thomas Baldwin


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