Molecular chaperones in the life cycle of proteins : structure, function, and mode of action
Author(s)
Bibliographic Information
Molecular chaperones in the life cycle of proteins : structure, function, and mode of action
Marcel Dekker, c1998
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Note
Includes bibliographical references and index
Description and Table of Contents
Description
Considers the integral role of molecular chaperones at different stages of a protein's life cycle. The text focuses on the biophysical, structural and functional properties of molecular chaperones, providing a biophysical view of chaperone problems useful in in vivo and in vitro studies, and augmenting current understanding of molecular chaperones as facilitators of de novo protein synthesis and recombinant protein folding.
Table of Contents
- Folding of monomeric proteins In Vitro: physicochemical and biological roles of the intermediate states
- oligomeric proteins
- chaperon interactions with nascent and newly synthesized proteins
- structure and properties of the 70-kilodalton heat-shock proteins
- the Hsp70 reaction cycle and its role in protein folding
- substrate-binding specification of the Hsp70 family
- major heat-shock chaperons in protein folding and inclusion body formation
- structure and function of the 90-kDa stress protein Hsp90
- Hsp104
- involvement of Hsp47 in the folding and processing of procollagen in the endoplasmic reticulum
- DnaJ proteins
- some structural aspects of chaperoning-assisted folding by GroEL and GroES
- a chaperoning from a thermophilic bacterium, thermos thermophilus
- protein disulphide isomerase
- catalysis of protein folding by propyl isomerases
- assembly of oligomers and multisubunit structures
- early events in the biosynthesis of secretory pathway proteins - role of molecular chaperons
- roles of molecular chaperons in mitochondrial protein import
- protein folding mediated by intramolecular chaperons
- molecular chaperons and intracellular protein degradation with emphasis on a selective lysosomal pathway of proteolysis
- proteasomes - the protein death machinery
- structure and function of small heat-shock protein
- aggregation and accessory proteins in the pathology of protein-folding diseases.
by "Nielsen BookData"
