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Synopsis
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.
- The readers will benefit from being provided with an in-depth overview of the physical concepts that govern different aspects of protein folding, disorder and self-assembly. By emphasizing the relationship between these issues, the approach adds a holistic character to the book
- The book is to a major extent mathematically based. Mathematics is part of the language of physicists and physical chemists which cannot be properly substituted by words
- For instructors, the book will offer a unique source for her/his teaching of current protein physics issues
- The way how the book will be constructed (multiple references to primary literature with DOI links, literature-based problem sets and topics for discussion) will facilitate a learning process suitable for research-oriented students
- Problem solving frequently requires the writing of short computer programs, something that is underemphasized in chemistry and biochemistry education (with the exception of computationally trained students, of course)
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About the Author
Reinhard Schweitzer-Stenner is a vibrational spectroscopist and biophysical chemist whose research focuses on the structure, dynamics, and function of biological molecules. Over a career spanning more than 40 years, he has combined spectroscopic, theoretical, and computational approaches to investigate heme proteins, peptides, and other complex biomolecular systems, contributing to advances in molecular spectroscopy, biophysics, and physical chemistry. He is Emeritus Professor of Chemistry at Drexel University, where he served on the faculty for nearly two decades, becoming Full Professor in 2009 before retiring in 2022 and remaining research active. His international academic career has included appointments in Germany, Puerto Rico, and the United States, including at Universität Bremen, where he received his habilitation in 1990, the University of Michigan, Ann Arbor, and the University of Puerto Rico, Río Piedras, before joining Drexel in 2003. His teaching has covered biophysics, spectroscopy, physical chemistry, atomic and molecular physics, statistical thermodynamics, and bioinorganic chemistry at undergraduate and graduate level, reflecting a rare breadth across the physical and biological chemistry interface.
From the Back Cover
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.
"About this title" may belong to another edition of this title.
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The Physics of Protein Structure and Dynamics: When and Why Proteins Fold or Don't Fold
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