The Physics of Protein Structure and Dynamics looks at various aspects of protein structure and dynamics from a physico-chemical point of view. It goes into some depth regarding the description of non-covalent forces that determine the relative stability of folded and unfolded proteins. Anharmonic protein dynamics involving motions between different minima of a rugged Gibbs energy landscape is described in great detail. The book combines various aspects of the protein folding/unfolding processes with an overview of intrinsically disordered proteins, which have attracted considerable interest of the protein community over the last 25 years but are thus far underrepresented in classroom-oriented textbooks. The book looks at protein folding and intrinsically disordered proteins as heavily interrelated topics that need to be viewed together. Furthermore, it presents some basic physico-chemical aspects of protein/peptide self-assembly into nanoscale fibrils. Intrinsically disordered peptides and proteins play a major role particularly in aggregation and self-assembly processes that lead to various diseases (Alzheimer, Parkinson, Huntington, Mad-Cow). Therefore, the relevance of protein disorder for protein self-assembly deserves a closer look. Protein self-assembly cannot be separated from protein folding since it is frequently the product of misfolding. With regard to modern theories, the folding processes are linked to insights on protein dynamics and the discovered relationship between proteins and spin glasses.
Table of Contents
1. Introduction 2. Intramolecular and Intermolecular Interactions 3. Protein Dynamics 4. Protein Folding and Unfolding 5. Intrinsically disordered proteins and poly-peptides 6. Misfolding and peptide/protein aggregation 7. Summary and Outlook
Authors
Reinhard Schweitzer-Stenner Professor of Chemistry, Drexel University, Philadelphia, USA. Research Background: Over the last forty years the author has conducted research in various areas of modern biophysical chemistry: (1) Structure and function of heme proteins studied mostly with resonance Raman spectroscopy, (2) Folding and unfolding of cytochrome c in solution and anionic surfaces, (3) Ligand-receptor binding as a trigger of mast cell and basophil activation, (4) Vibrational dynamics of peptides, (5) Conformational analysis of peptides used as model systems for unfolded and disordered proteins, (6) Aggregation, self-assembly and gelation of short and ultrashort peptidesPublication record: 211 peer reviewed papers and book articles; he is the editor of the book: Protein and Peptide Folding, Misfolding and Non-Folding, Wiley and Sons, ISBN 978-0-470-59169-7
Teaching experience: Over the last 40 years has taught classes in biophysics, biophysical chemistry, atomic and molecular physics, spectroscopy, statistical thermodynamics and bioinorganic chemistry on the undergraduate and graduate level
