Protein and Peptide Folding, Misfolding, and Non-Folding
Protein and Peptide Folding, Misfolding, and Non-Folding

Author: Reinhard Schweitzer-Stenner

Publisher: John Wiley & Sons

Published: 2012-02-08

Total Pages: 484

ISBN-13: 1118183355

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Sheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseases With the discovery of intrinsically disordered proteins and peptides (IDPs), researchers realized that proteins do not necessarily adopt a well defined secondary and tertiary structure in order to perform biological functions. In fact, IDPs play biologically relevant roles, acting as inhibitors, scavengers, and even facilitating DNA/RNA-protein interactions. Due to their propensity for self-aggregation and fibril formation, some IDPs are involved in neurodegenerative diseases such as Parkinson's and Alzheimer's. With contributions from leading researchers, this text reviews the most recent studies, encapsulating our understanding of IDPs. The authors explain how the growing body of IDP research is building our knowledge of the folding process, the binding of ligands to receptor molecules, and peptide self-aggregation. Readers will discover a variety of experimental, theoretical, and computational approaches used to better understand the properties and function of IDPs. Moreover, they'll discover the role of IDPs in human disease and as drug targets. Protein and Peptide Folding, Misfolding, and Non-Folding begins with an introduction that explains why research on IDPs has significantly expanded in the past few years. Next, the book is divided into three sections: Conformational Analysis of Unfolded States Disordered Peptides and Molecular Recognition Aggregation of Disordered Peptides Throughout the book, detailed figures help readers understand the structure, properties, and function of IDPs. References at the end of each chapter serve as a gateway to the growing body of literature in the field. With the publication of Protein and Peptide Folding, Misfolding, and Non-Folding, researchers now have a single place to discover IDPs, their diverse biological functions, and the many disciplines that have contributed to our evolving understanding of them.

The Physics of Protein Structure and Dynamics
The Physics of Protein Structure and Dynamics

Author: Reinhard Schweitzer-Stenner

Publisher: Elsevier

Published: 2024-09-23

Total Pages: 328

ISBN-13: 0443159653

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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)

Fuzziness
Fuzziness

Author: Monika Fuxreiter

Publisher: Springer Science & Business Media

Published: 2012-03-07

Total Pages: 210

ISBN-13: 1461406595

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Detailed characterization of fuzzy interactions will be of central importance for understanding the diverse biological functions of intrinsically disordered proteins in complex eukaryotic signaling networks. In this volume, Peter Tompa and Monika Fuxreiter have assembled a series of papers that address the issue of fuzziness in molecular interactions. These papers provide a broad overview of the phenomenon of fuzziness and provide compelling examples of the central role played by fuzzy interactions in regulation of cellular signaling processes and in viral infectivity. These contributions summarize the current state of knowledge in this new field and will undoubtedly stimulate future research that will further advance our understanding of fuzziness and its role in biomolecular interactions.

Protein Physics
Protein Physics

Author: Alexei V. Finkelstein

Publisher: Elsevier

Published: 2016-06-22

Total Pages: 530

ISBN-13: 0081012365

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Protein Physics: A Course of Lectures covers the most general problems of protein structure, folding and function. It describes key experimental facts and introduces concepts and theories, dealing with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states. The book systematically summarizes and presents the results of several decades of worldwide fundamental research on protein physics, structure, and folding, describing many physical models that help readers make estimates and predictions of physical processes that occur in proteins. New to this revised edition is the inclusion of novel information on amyloid aggregation, natively disordered proteins, protein folding in vivo, protein motors, misfolding, chameleon proteins, advances in protein engineering & design, and advances in the modeling of protein folding. Further, the book provides problems with solutions, many new and updated references, and physical and mathematical appendices. In addition, new figures (including stereo drawings, with a special appendix showing how to use them) are added, making this an ideal resource for graduate and advanced undergraduate students and researchers in academia in the fields of biophysics, physics, biochemistry, biologists, biotechnology, and chemistry. - Fully revised and expanded new edition based on the latest research developments in protein physics - Written by the world's top expert in the field - Deals with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states - Summarizes, in a systematic form, the results of several decades of worldwide fundamental research on protein physics and their structure and folding - Examines experimental data on protein structure in the post-genome era

Mechanisms of Protein Folding
Mechanisms of Protein Folding

Author: Roger H. Pain

Publisher: Oxford University Press, USA

Published: 2000

Total Pages: 433

ISBN-13: 9780199637881

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Since the publication of the first edition of mechanisms of protein folding in 1994, significant advances in both the technical and conceptual understanding of protein folding. This new edition has been brought up to date in content, context, and authorship and will make the subject accessibleto a wide range of scientists. The emphasis on experimental approaches has benn maintained from the first edition but this time within the explicit context of simulations and energy surfaces. There is an introductory chapter explaining the 'new' model of protein folding, which takes into account theheterogeneity of the starting state. Advances in interpreting observed kinetic data and the development of technology to observe fast folding reactions and characterize intermediate structures have accompanied this new view and are covered in detail. The term 'molten globule'is often usedincorrectly but here the significance of the term is carefully described at different satges of folding. The concept of the transition state, including the complementary approaches of molecular dynamics and protein engineering, is also discussed in detail. In vitro studies provide the molecularbasis for the thermodynamic and kinetic energy minimization of the in vivo processes of protein folding and two of the potentially rate determining reactions are disulphide bond formation and proline isomerization. It has also become increasingly apparent that chaperone proteins play a vital role inprotein folding and other reactions of proteins involoving major conformational change and the molecular details of these processes are discussed in detail in chapter 14. The final chapter describes the centreal importance of protein folding and unfolding reactions in disease and gives claerdefinition of the term 'misfolding'. Studying protein folding in vivo is full of problems and to show how these problems can be overcome in practice, three case studies of three very different types of protein have been included: the small globular protein apomyoglobin; the fibrous protein collagen;and the membrane protein haemagglutinin.

Protein Folding, Misfolding and Aggregation
Protein Folding, Misfolding and Aggregation

Author: Victor Muñoz

Publisher: Royal Society of Chemistry

Published: 2008-06-24

Total Pages: 289

ISBN-13: 1847558283

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Protein folding and aggregation is the process by which newly synthesized proteins fold into the specific three-dimensional structures defining their biologically active states. It has always been a major focus of research in biochemistry and has often been seen as the unsolved second part of the genetic code. In the last 10 years we have witnessed a quantum leap in the research in this exciting area. Computational methods have improved to the extent of making possible to simulate the complete folding process of small proteins and the early stages of protein aggregation. Experimental methods have evolved to permit resolving fast processes of folding reactions and visualizing single molecules during folding. The findings from these novel experiments and detailed computer simulations have confirmed the main predictions of analytical theory of protein folding. In summary, protein folding research has finally acquired the status of a truly quantitative science, paving the way for more exciting developments in the near future. This unique book covers all the modern approaches and the many advances experienced in the field during the last 10 years. There is also much emphasis on computational methods and studies of protein aggregation which have really flourished in the last decade. It includes chapters in the areas that have witnessed major developments and are written by top experts including:computer simulations of folding, fast folding, single molecule spectroscopy, protein design, aggregation studies (both computational and experimental). Readers will obtain a unique perspective of the problems faced in the biophysical study of protein conformational behaviour in aqueous solution and how these problems are being solved with a multidisciplinary approach that combines theory, experiment and computer simulations. Protein Folding, Misfolding and Aggregation Classical Themes and Novel Approaches is essential reading for graduate students actively involved in protein folding research, other scientists interested in the recent progress of the field and instructors revamping the protein folding section of their biochemistry and biophysics courses.

Protein Oxidation and Aging
Protein Oxidation and Aging

Author: Tilman Grune

Publisher: John Wiley & Sons

Published: 2012-11-07

Total Pages: 494

ISBN-13: 111849301X

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Reviews our current understanding of the role of protein oxidation in aging and age-related diseases Protein oxidation is at the core of the aging process. Setting forth a variety of new methods and approaches, this book helps researchers conveniently by exploring the aging process and developing more effective therapies to prevent or treat age-related diseases. There have been many studies dedicated to the relationship between protein oxidation and age-related pathology; now it is possible for researchers and readers to learn new techniques as utilizing protein oxidation products as biomarkers for aging. Protein Oxidation and Aging begins with a description of the tremendous variety of protein oxidation products. Furthermore, it covers: Major aspects of the protein oxidation process Cellular mechanisms for managing oxidized proteins Role of protein oxidation in aging Influence of genetic and environmental factors on protein oxidation Measuring protein oxidation in the aging process Protein oxidation in age-related diseases References at the end of each chapter serve as a gateway to the growing body of original research studies and reviews in the field.

Tau oligomers
Tau oligomers

Author: Jesus Avila

Publisher: Frontiers E-books

Published: 2014-08-18

Total Pages: 114

ISBN-13: 288919261X

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Neurofibrillary tangles (NFTs) composed of intracellular aggregates of tau protein are a key neuropathological feature of Alzheimer’s Disease (AD) and other neurodegenerative diseases, collectively termed tauopathies. The abundance of NFTs has been reported to correlate positively with the severity of cognitive impairment in AD. However, accumulating evidences derived from studies of experimental models have identified that NFTs themselves may not be neurotoxic. Now, many of tau researchers are seeking a “toxic” form of tau protein. Moreover, it was suggested that a “toxic” tau was capable to seed aggregation of native tau protein and to propagate in a prion-like manner. However, the exact neurotoxic tau species remain unclear. Because mature tangles seem to be non-toxic component, “tau oligomers” as the candidate of “toxic” tau have been investigated for more than one decade. In this topic, we will discuss our consensus of “tau oligomers” because the term of “tau oligomers” [e.g. dimer (disulfide bond-dependent or independent), multimer (more than dimer), granular (definition by EM or AFM) and maybe small filamentous aggregates] has been used by each researchers definition. From a biochemical point of view, tau protein has several unique characteristics such as natively unfolded conformation, thermo-stability, acid-stability, and capability of post-translational modifications. Although tau protein research has been continued for a long time, we are still missing the mechanisms of NFT formation. It is unclear how the conversion is occurred from natively unfolded protein to abnormally mis-folded protein. It remains unknown how tau protein can be formed filaments [e.g. paired helical filament (PHF), straight filament and twisted filament] in cells albeit in vitro studies confirmed tau self-assembly by several inducing factors. Researchers are still debating whether tau oligomerization is primary event rather than tau phosphorylation in the tau pathogenesis. Inhibition of either tau phosphorylation or aggregation has been investigated for the prevention of tauopathies, however, it will make an irrelevant result if we don’t know an exact target of neurotoxicity. It is a time to have a consensus of definition, terminology and methodology for the identification of “tau oligomers”.

Protein Misfolding, Aggregation and Conformational Diseases
Protein Misfolding, Aggregation and Conformational Diseases

Author: Vladimir N. Uversky

Publisher: Springer Science & Business Media

Published: 2007-05-26

Total Pages: 538

ISBN-13: 0387365346

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The second volume continues to fill the gap in protein review and protocol literature. It does this while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. The focus of Part B is the molecular basis of differential disorders.

Protein Families
Protein Families

Author: Christine A. Orengo

Publisher: John Wiley & Sons

Published: 2014-02-03

Total Pages: 566

ISBN-13: 0470624221

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New insights into the evolution and nature of proteins Exploring several distinct approaches, this book describes the methods for comparing protein sequences and protein structures in order to identify homologous relationships and classify proteins and protein domains into evolutionary families. Readers will discover the common features as well as the key philosophical differences underlying the major protein classification systems, including Pfam, Panther, SCOP, and CATH. Moreover, they'll discover how these systems can be used to understand the evolution of protein families as well as understand and predict the degree to which structural and functional information are shared between relatives in a protein family. Edited and authored by leading international experts, Protein Families offers new insights into protein families that are important to medical research as well as protein families that help us understand biological systems and key biological processes such as cell signaling and the immune response. The book is divided into three sections: Section I: Concepts Underlying Protein Family Classification reviews the major strategies for identifying homologous proteins and classifying them into families. Section II: In-Depth Reviews of Protein Families focuses on some fascinating super protein families for which we have substantial amounts of sequence, structural and functional data, making it possible to trace the emergence of functionally diverse relatives. Section III: Review of Protein Families in Important Biological Systems examines protein families associated with a particular biological theme, such as the cytoskeleton. All chapters are extensively illustrated, including depictions of evolutionary relationships. References at the end of each chapter guide readers to original research papers and reviews in the field. Covering protein family classification systems alongside detailed descriptions of select protein families, this book offers biochemists, molecular biologists, protein scientists, structural biologists, and bioinformaticians new insight into the evolution and nature of proteins.