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  • M9937 - Mechanisms of Protein Folding, 2nd ed.

M9937 Sigma

Mechanisms of Protein Folding, 2nd ed.

  •  ISBN-10 0-19-963788-1

  •  ISBN-13 978-0-19-963788-1



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publication info   R.H. Pain, ed., Oxford University Press, 2000, 480 pp., soft cover
mfr. no.   Oxford University Press


General description

Process by which polypeptide chains become their final 3-dimensional protein forms is clearly explained. Second edition incorporates significant improvements such as advances in interpreting observed kinetic data, development of technology to observe fast folding reactions, molten globule state, and vital role of chaperone proteins in protein folding. New discoveries of the central importance of protein folding and unfolding reactions in biology and medicine, including mutation and misfolding, are explored. Three case studies elucidate the difficulties of studying protein folding in vivo.

Table of Contents

1. The nature and significance of protein folding, Christopher M. Dobson
2. Kinetic models in protein folding, Oliver Bieri and Thomas Kiefhaber
3. Early stages of protein folding, Heinrich Roder, Gülner A. Elöve, and M. C. Ramachandra Shastry
4. Protein folding monitored by mass spectrometry, Carol V. Robinson
5. Folding events in the submillisecond range, Martin Gruebele
6. The molten globule state: the physical picture and biological significance, Kunihiro Kuwajima and Munehito Arai
7. Transition states in protein folding, Valerie Daggett and Alan R. Fersht
8. Proline isomerization and its catalysis in protein folding, Jochen Balbach and Franz X. Schmid
9. Protein folding coupled to disulphide-bond formation, Thomas E. Creighton
10. Assembly of multi-subunit structures, Robert Seckler
11. Case study 1: The folding process of apomyoglobin, Peter E. Wright and Robert L. Baldwin
12. Case study 2: Folding of the collagen triple-helix and its naturally occurring mutants, Jean Baum and Barbara Brodsky
13. Case study 3: Folding of influenza haemagglutinin in the living cell, Lars Ellgaard and Ari Helenius
14. Cellular functions of molecular chaperones, Michel R. Leroux and F. Ulrich Hartl
15. Protein folding and human disease, Stephen W. Raso and Jonathan King

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