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.
- Hardback | 323 pages
- 166.9 x 231.9 x 28.2mm | 1,469.65g
- 01 Apr 1996
- Elsevier Science Publishing Co Inc
- Academic Press Inc
- San Diego, United States
About R. J. Ellis
Ian Cameron is Reader in Chemical Engineering at the University of Queensland with teaching, research, and consultancy interests in process systems engineering. He has a particular interest in process modeling, dynamic simulation, and the application of advanced numerical methods to large-scale process systems. He has developed innovative courses in process modeling, design, and risk management, having extensive industrial experience in these areas. He continues to work closely with industry and government on systems approaches to process and risk management problems, as well as the development of internet-based tools for process systems applications.
Table of contents
Chaperonins - introductory perspective, R.J. Ellis; evolutionary relationships of chaperonins, R.S. Gupta; chaperonins of photosynthetic organisms, A.A. Gatenby; chaperonin-mediated folding and assembly of proteins in mitochondria, T. Langer and W. Neupert; structure and function of chapronins in archaebacteria and eukaryotic cytosol, K.R. Willison and A.L. Horwich; regulation of chaperonin gene expression, S.M. Van der Veis and C. Georgopoulus; kinetic and energetic aspects of chaperonin function, A.R. Clarke and P.A. Lind; role of prokaryotic chaperonins in protein folding, J. Martin et al; chaperonin structure and conformational changes, H.R. Saibil; immunological aspects of chaperonins, A.R.M. Coates.