Molecular Chaperones by John N. Abelson

Molecular Chaperones

byJohn N. AbelsonEditorMelvin I. Simon, George H. Lorimer

Hardcover | March 5, 1998

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The critically acclaimed laboratory standard for more than forty years,Methods in Enzymologyis 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.

  • 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

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Title:Molecular ChaperonesFormat:HardcoverDimensions:500 pages, 9 × 6 × 0.98 inPublished:March 5, 1998Publisher:Academic Press

The following ISBNs are associated with this title:

ISBN - 10:0121821919

ISBN - 13:9780121821913

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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-DeficientEscherichia coliCell-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 inEscherichia 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 forEscherichia 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 fromChromatium vinosum.
F.R. Tabita, W.T. Lee, and G.M.F. Watson, Chaperonins of Purple Nonsulfur BacteriumRhodobacter sphaeroides.
R.K. Scopes and K. Truscott, Chaperonins fromThermoanaerobacterSpecies.
M. Yoshida and H. Taguchi, Chaperonin from a Thermophile,Thermus thermophilus.
M. Morioka and H. Ishikawa, Insect Chaperonin 60: Symbionin.
G. Schatz, Y. Dubaquié, and S. Rospert, Purification of Yeast Mitochondrial Chaperonin 60 and Co-Chaperonin 10.
P.V. Viitanen, G. Lorimer, W. Bergmeier, C. Weiss, M. Kessel, and P. Goloubinoff, Purification of Mammalian Mitochondrial Chaperonin 60 throughin vitroReconstitution of Active Oligomers.
P.V. Viitanen, K. Bacot, R. Dickson, and T. Webb, Purification of Recombinant Plant and Animal GroES Homologs: Chloroplast and Mitochondrial Chaperonin 10.
N.J. Cowan, Mammalian Cytosolic Chaperonin.
H.R. Saibil, S. Chen, and A.M. Roseman, Electron Microscopy of Chaperonins.
P. Goloubinoff, A. Azem, and C. Weiss, Using Chemical Cross-linking Structural Analysis of GroE Chaperonin Complexes.
H-J. Schönfeld and J. Behlke, Molecular Chaperones and Their Interactions Investigated by Analytical Ultracentrifugation and Other Methodologies.
S.E. Radford, C.V. Robinson, and M. Gross, Probing Conformation of GroEL-Bound Substrate Proteins by Mass Spectrometry.
P.M. Horowitz and B.M. Gorovits, Fluorescence Anisotropy Method for Investigation of GroEL-GroES Interaction.
J.W. Seale, B.T. Brazil, and P.M. Horowitz, Photoincorporation of Fluorescent Probe into GroEL: Defining Site of Interaction.
J. Buchner, H. Grallert, and U. Jakob, Analysis of Chaperone Function Using Citrate Synthase as Nonnative Substrate Protein.
J. Buchner, M. Ehrnsperger, M. Gaestel, and S. Walke, Purification and Characterization of Small Heat Shock Proteins.
G.J. Lee and E. Vierling, Expression, Purification, and Molecular Chaperone Activity Plant Recombinant Small Heat Shock Proteins.
J. Horwitz, Q-L. Huang, L. Ding, and M.P. Bova, Lens a-Crystallin: Chaperone-like Properties.
S. Blond, M. Chevalier, and L. King, Purification and Properties of BiP.
J. Buchner, S. Bose, and U. Jakob, Purification and Characterization of Prokaryotic and Eukaryotic Hsp 90.
J. Buchner, T. Weikl, H. Bügl, F. Pirkl, and S. Bose, Purification of Hsp90 Partner Proteins Hop/p60, p23, and FKBP52.
S. Lindquist and E.C. Schirmer, Purification and Properties of Hsp104 from Yeast.
L.L. Randall, T.B. Topping, V.F. Smith, D.L. Diamond, and S.J.S. Hardy, SecB: A Chaperone fromEscherichia coli.
Author Index.
Subject Index.

Editorial Reviews

Praise for the Series"The Methods in Enzymology series represents the gold-standard."--NEUROSCIENCE"Incomparably useful." --ANALYTICAL BIOCHEMISTRY"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." --BIO/TECHNOLOGY"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." --CHEMISTRY IN INDUSTRY"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." --AMERICAN SOCIETY OF MICROBIOLOGY NEWS"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." --ENZYMOLOGIA"A series that has established itself as a definitive reference for biochemists." --JOURNAL OF CHROMATOGRAPHY