The first of its kind, this volume presents the latest research findings on the chaperonins, the best studied family of a class of proteins known as molecular chaperones. These findings are changing our view of some fundamental cellular processes involving proteins, especially how proteins fold into their functional conformations.

Key Features

@introbul:Key Features @bul:* Origins of the new view of protein folding * Prokaryotic chaperonins * Eukaryotic chaperonins * Evolution of the chaperonins * Refolding of denatured proteins * Organelle biosynthesis * Biomedical aspects

Table of Contents

R.J. Ellis, Chaperonins: Introductory Perspective. R.S. Gupta, Evolutionary Relationships of Chaperonins. A.A. Gatenby, Chaperonins of Photosynthetic Organisms. T. Langer and W. Neupert, Chaperonin-Mediated Folding and Assembly of Proteins in Mitochondria. K.R. Willison and A.L. Horwich, Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol. S.M. Van Der Veis and C. Georgopoulos, Regulation of Chaperonin Gene Expression. A.R. Clarke and P.A. Lund, Kinetic and Energetic Aspects of Chaperonin Function. J. Martin, M. Mayhew and F. Ulrich-Hartl, Role of Prokaryotic Chaperonins in Protein Folding. H.R. Saibil, Chaperonin Structure and Conformational Changes. A.R.M. Coates, Immunological Aspects of Chaperonins. Subject Index.


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© 1996
Academic Press
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