Protein Folding Handbook
1. Edition January 2005
LXIV, 2559 Pages, Hardcover
644 Pictures (86 Colored Figures)
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.
Price: 1.970,00 €
Price incl. VAT, excl. Shipping
How a polypeptide chain folds into a stable and functional protein is probably the most important question in present-day molecular biology. Reliably predicting the folding process allows to deduce protein function from genomic information alone and will bring about a revolution in structural genomics. Understanding the way in which proper protein folding is controlled by the cell is required to find a cure for Alzheimer's and other diseases caused by misfolded proteins.
This unique handbook contains the expertise from more than 60 research groups, covering the entire range of topics in protein folding - from biophysics to molecular medicine.
The first part explains the principles and factors governing protein stability, and how this knowledge may be used to predict folding pathways. It also surveys important techniques used to study the protein folding process, including spectroscopic, chemical and biological techniques.
The second part is devoted to protein folding, unfolding, and misfolding in the cellular context, introducing chaperones and other enzymes involved in protein folding, as well as a study of the pathophysiology of misfolded proteins in amyloid and other disease states. The whole is rounded off by a discussion of the possibility of interfering with the protein folding process by genetic engineering.
The comprehensiveness and outstanding quality of the carefully selected contents make this the ultimate reference for every scientist with an interest in protein folding.
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
Polyglutamine repeat diseases
Protein refolding technology
Engineering protein stability
Folding of nascent polypeptides
Protein assembly processes
Journal of the American Chemical Society
Professor Buchner's research is centered on the folding process of proteins and its efficiency in vitro and in vivo. To improve the efficiency of protein production, he has pioneered the biotechnological use of chaperones and holds several patents in this area of research.
Thomas Kiefhaber is Professor of Biophysical Chemistry at the Biozentrum, University of Basel (Switzerland). He studied Biology at the University of Regensburg (Germany) and, after completing his PhD in Biophysical Chemistry, spent two years as a post-doc with R. L. Baldwin at Stanford University. Since 1993 he is a member of the faculty of Basel University and was named professor for Biophysical Chemistry in 1999.
Professor Kiefhaber's research is centered on the investigation of kinetics and mechanism of protein folding with biophysical methods.