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Molecular Chaperones
 
 

Molecular Chaperones, 1st Edition

 
Molecular Chaperones, 1st Edition,George Lorimer,Thomas Baldwin,ISBN9780121821913
 
 
 

Lorimer   &   Baldwin   

Abelson  &   Simon   

Academic Press

9780121821913

500

229 X 152

Print Book

Hardcover

In Stock

Estimated Delivery Time
USD 210.00
 
 

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

Description

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.

Readership

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

George Lorimer

Affiliations and Expertise

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

Thomas Baldwin

Molecular Chaperones, 1st Edition

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, 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 through in vitro Reconstitution 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 from Escherichia coli.
Author Index.
Subject Index.

Quotes and reviews

@from:Praise for the Series
@qu:"The Methods in Enzymology series represents the gold-standard."
@source:--NEUROSCIENCE
@qu:"Incomparably useful."
@source:--ANALYTICAL BIOCHEMISTRY
@qu:"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."
@source:--BIO/TECHNOLOGY
@qu:"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."
@source:--CHEMISTRY IN INDUSTRY
@qu:"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."
@source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
@qu:"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."
@source:--ENZYMOLOGIA
@qu:"A series that has established itself as a definitive reference for biochemists."
@source:--JOURNAL OF CHROMATOGRAPHY
 
 
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