The Physics of Protein Structure and Dynamics
When and Why Proteins Fold or Don’t Fold
- 1st Edition - September 23, 2024
- Author: Reinhard Schweitzer-Stenner
- Language: English
- Paperback ISBN:9 7 8 - 0 - 4 4 3 - 1 5 9 6 4 - 0
- eBook ISBN:9 7 8 - 0 - 4 4 3 - 1 5 9 6 5 - 7
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… Read more
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Request a sales quoteThe 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)
Graduate level classes and above that focus on the biophysics of proteins. The book should be useful for courses in physics, chemistry, biophysics and biochemistry programs. It deliberately puts a larger emphasis on physical concepts and mathematics than many biophysics books. The book could also be useful for programs in biological and biomedical engineering. In research groups involved in studies of protein folding and intrinsically disordered proteins the book could be added to the basic literature beginning graduate students should read prior to prepare themselves for their research project. Graduate students and more senior researchers will use the book alike if the reading and understanding of a research article requires them to re-familiarize themselves with important biophysical concepts
- Title of Book
- Cover image
- Title page
- Table of Contents
- Copyright
- About the author
- Preface
- Chapter 1 Intra and intermolecular interactions
- Abstract
- 1.1 Introduction
- 1.2 Hydrogen bonding
- 1.3 Electrostatic interactions and salt bridges
- 1.4 Van der Waals interactions
- 1.5 Protein (Peptide)-water interactions
- 1.6 Protein-metal interactions
- 1.7 Topics for discussion
- 1.8 Problems
- References
- Chapter 2 Protein dynamics
- Abstract
- 2.1 Introduction
- 2.2 General thoughts about structure and dynamics
- 2.3 Protein dynamics in the harmonic limit
- 2.4 Conformational substates and anharmonicities
- 2.5 Conformational motions in a rugged energy landscape
- 2.6 Ligand binding in Mb probes fluctuations and dissipation in a rugged landscape
- 2.7 Spin glasses
- 2.8 The role of the solvent, α- and β-relaxations
- 2.9 Conformational substates and functional properties
- 2.10 Chapter summary
- 2.11 Topics for discussion
- 2.12 Problems
- References
- Chapter 3 Protein folding and unfolding
- Abstract
- 3.1 Introduction
- 3.2 The folded state of proteins
- 3.3 The unfolded state of proteins
- 3.4 The thermodynamics of protein folding and unfolding
- 3.5 The formation of secondary structures
- 3.6 Kinetic aspects of protein folding and unfolding
- 3.7 The energy landscape model
- 3.8 Protein folding in crowded environment
- 3.9 Unanswered questions
- 3.10 Topics for discussions
- 3.11 Problems
- References
- Chapter 4 Intrinsically disordered proteins
- Abstract
- 4.1 Introduction
- 4.2 Conformational propensities
- 4.3 Conformational propensities and solvation
- 4.4 Charge distributions and solvation
- 4.5 Characterizing the conformational ensembles of intrinsically disordered proteins
- 4.6 Order→disorder and disorder→disorder transitions
- 4.7 Topics for discussion
- 4.8 Problems
- References
- Chapter 5 Protein and peptide self-assembly
- Abstract
- 5.1 Introduction
- 5.2 Amyloid structure and underlying forces
- 5.3 Kinetics of amyloid formation
- 5.4 Liquid–liquid demixing
- 5.5 Outlook
- 5.6 Topics of discussion
- 5.7 Problems
- References
- Chapter 6 Summary and outlook
- Abstract
- References
- Index
- No. of pages: 326
- Language: English
- Edition: 1
- Published: September 23, 2024
- Imprint: Academic Press
- Paperback ISBN: 9780443159640
- eBook ISBN: 9780443159657
RS
Reinhard Schweitzer-Stenner
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 peptides
Publication 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
Affiliations and expertise
Professor of Chemistry, Drexel University, Philadelphia, USARead The Physics of Protein Structure and Dynamics on ScienceDirect