1. Edition - January 2005
1270.- Euro
2005. LXIV, 2559 Pages, 5 Volumes, Hardcover
644 Fig. (86 Colored Fig.), 86 Tab. 
- Handbook/Reference Book -
ISBN-10: 3-527-30784-2
ISBN-13: 978-3-527-30784-5 - Wiley-VCH, Weinheim







Sample Chapter



Short description
This comprehensive handbook contains the carefully selected expertise from more than 70 research groups. The first part explains the principles and factors governing protein stability, and how these may be used to predict folding pathways. The second is devoted to protein folding, unfolding, and misfolding in the cellular context, as well as the pathophysiology of misfolded proteins in amyloid and other disease states. The whole is rounded off by a discussion of possible interference by genetic engineering.
The ultimate reference for every scientist with an interest in protein folding.


From the contents
PART I: Principles of Protein Folding and Stability (partial contents)
Spectroscopic techniques to study protein folding and stability
Solvent effects on protein stability
Analysis of protein folding kinetics, kinetic mechanisms, transition states
Single molecule protein folding
Dynamics of unfolded polypeptide chains
Folding and stability of oligomeric proteins
Folding of membrane proteins
Molecular dynamics simulations of folding and unfolding
Ab initio methods for protein structure prediction

PART II: Protein Misfolding, Molecular Chaperones and Folding Catalysts (partial contents)
Methods to study aggregate formation
Amyloid diseases
Polyglutamine repeat diseases
Protein refolding technology
Engineering protein stability
Chaperone machines
Folding of nascent polypeptides
Protein assembly processes