Protein Folding

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C. M. Dobson, A. R. Fersht
Cambridge University Press, Aug 8, 1996 - Science - 119 pages
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The ability of proteins to fold rapidly and efficiently into intricate and highly specific structures following their synthesis on ribosomes is an essential part of the conversion of genetic information into cellular activity. However, little is understood in detail of how this occurs. The Royal Society meeting on which this volume is based focused on the molecular basis of the folding processes and brought together a wide range of leading experimental and theoretical scientists in this field. This volume offers an authoritative collection of the foundations of current work. The first section discusses the experimental elucidation of the pathways of protein folding. The second section looks at theoretical approaches to folding, and the final group addresses the issue of how proteins fold in vivo. This volume will be of value to all those with an interest in protein folding, especially those in molecular biology, biochemistry and cell biology.
 

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Contents

Disulphidecoupled protein folding pathways
5
delineation of pathways at high resolution
11
studies of lysozyme and 𝛼lactalbumin
17
Initial studies of the equilibrium folding pathway of staphylococal nuclease
27
Kinetic and equilibrium folding intermediates
35
Does the molten globule have a nativelike tertiary fold?
43
Investigation of protein unfolding and stability by computer simulation
49
Models of cooperativity in protein folding
61
towards understanding folding from inspection of native structures
71
Design of twostranded and threestranded coiledcoil peptides
81
folding and chaperone interaction during elongation on ribosomes
89
Folding and association versus misfolding and aggregation of proteins
97
Principles of chaperonemediated protein folding
107
structure and functional implications
113
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