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Author: James D. Gunton
Publisher: Cambridge University Press
ISBN: 9781107424272
Category : Science
Languages : en
Pages : 394
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Book Description
The quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of this book is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of the book deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring. The book, containing color plate sections, is suitable for graduate students and academic researchers in physics, chemistry, structural biology, protein crystallography and medicine.
Author: Vladimir N. Uversky
Publisher: Springer Science & Business Media
ISBN: 0387365346
Category : Medical
Languages : en
Pages : 538
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Book Description
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.
Author: James D. Gunton
Publisher: Cambridge University Press
ISBN: 9781107424272
Category : Science
Languages : en
Pages : 394
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Book Description
The quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of this book is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of the book deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring. The book, containing color plate sections, is suitable for graduate students and academic researchers in physics, chemistry, structural biology, protein crystallography and medicine.
Author: Jennifer J. McManus
Publisher: Humana
ISBN: 9781493996803
Category : Science
Languages : en
Pages : 266
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Book Description
This volume explores experimental and computational approaches to measuring the most widely studied protein assemblies, including condensed liquid phases, aggregates, and crystals. The chapters in this book are organized into three parts: Part One looks at the techniques used to measure protein-protein interactions and equilibrium protein phases in dilute and concentrated protein solutions; Part Two describes methods to measure kinetics of aggregation and to characterize the assembled state; and Part Three details several different computational approaches that are currently used to help researchers understand protein self-assembly. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Thorough and cutting-edge, Protein Self-Assembly: Methods and Protocols is a valuable resource for researchers who are interested in learning more about this developing field.
Author: Irena Roterman-Konieczna
Publisher: Elsevier
ISBN: 0081029829
Category : Medical
Languages : en
Pages : 280
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Book Description
From Globular Proteins to Amyloids proposes a model and mechanism for explaining protein misfolding. Concepts presented are based on a model originally intended to show how proteins attain their native conformations. This model is quantitative in nature and founded upon arguments derived from information theory. It facilitates prediction and simulation of the amyloid fibrillation process, also identifying the progressive changes that occur in native proteins that lead to the emergence of amyloid aggregations. - Introduces basic rules for protein folding, along with the conditions that result in misfolding - Presents research that lies in treating the aqueous environment as a continuum rather than a set of individual water molecules (i.e. the classic representation) - Provides practical applications for helping the prevention of amyloidosis and improving drug design
Author: Irena Roterman-Konieczna
Publisher: Elsevier
ISBN: 1908818255
Category : Science
Languages : en
Pages : 241
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Book Description
Protein folding is a process by which a protein structure assumes its functional shape of conformation, and has been the subject of research since the publication of the first software tool for protein structure prediction. Protein folding in silico approaches this issue by introducing an ab initio model that attempts to simulate as far as possible the folding process as it takes place in vivo, and attempts to construct a mechanistic model on the basis of the predictions made. The opening chapters discuss the early stage intermediate and late stage intermediate models, followed by a discussion of structural information that affects the interpretation of the folding process. The second half of the book covers a variety of topics including ligand binding site recognition, the "fuzzy oil drop" model and its use in simulation of the polypeptide chain, and misfolded proteins. The book ends with an overview of a number of other ab initio methods for protein structure predictions and some concluding remarks. - Discusses a range of ab initio models for protein structure prediction - Introduces a unique model based on experimental observations - Describes various methods for the quantitative assessment of the presented models from the viewpoint of information theory
Author: Alexei V. Finkelstein
Publisher: Elsevier
ISBN: 0081012365
Category : Science
Languages : en
Pages : 530
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Book Description
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
Author: Richard I. Morimoto
Publisher:
ISBN: 9781936113064
Category : Biological transport
Languages : en
Pages : 0
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Book Description
Proper folding of proteins is crucial for cell function. Chaperones and enzymes that post-translationally modify newly synthesized proteins help ensure that proteins fold correctly, and the unfolded protein response functions as a homeostatic mechanism that removes misfolded proteins when cells are stressed. This book covers the entire spectrum of proteostasis in healthy cells and the diseases that result when control of protein production, protein folding, and protein degradation goes awry.
Author: Jasim Ahmed
Publisher: John Wiley & Sons
ISBN: 1118935721
Category : Technology & Engineering
Languages : en
Pages : 490
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Book Description
Glass and State Transitions in Food and Biological Materials describes how glass transition has been applied to food micro-structure, food processing, product development, storage studies, packaging development and other areas. This book has been structured so that readers can initially grasp the basic principles and instrumentation, before moving through the various applications. In summary, the book will provide the “missing link” between food science and material science/polymer engineering. This will allow food scientists to better understand the concept and applications of thermal properties.
Author: Daniel John Rigden
Publisher: Springer Science & Business Media
ISBN: 1402090587
Category : Science
Languages : en
Pages : 330
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Book Description
Proteins lie at the heart of almost all biological processes and have an incredibly wide range of activities. Central to the function of all proteins is their ability to adopt, stably or sometimes transiently, structures that allow for interaction with other molecules. An understanding of the structure of a protein can therefore lead us to a much improved picture of its molecular function. This realisation has been a prime motivation of recent Structural Genomics projects, involving large-scale experimental determination of protein structures, often those of proteins about which little is known of function. These initiatives have, in turn, stimulated the massive development of novel methods for prediction of protein function from structure. Since model structures may also take advantage of new function prediction algorithms, the first part of the book deals with the various ways in which protein structures may be predicted or inferred, including specific treatment of membrane and intrinsically disordered proteins. A detailed consideration of current structure-based function prediction methodologies forms the second part of this book, which concludes with two chapters, focusing specifically on case studies, designed to illustrate the real-world application of these methods. With bang up-to-date texts from world experts, and abundant links to publicly available resources, this book will be invaluable to anyone who studies proteins and the endlessly fascinating relationship between their structure and function.
Author: Jesus Avila
Publisher: Frontiers E-books
ISBN: 288919261X
Category : Medicine (General)
Languages : en
Pages : 114
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Book Description
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”.
